# |
PMID |
Sentence |
1 |
1701612
|
The effect of incorporating the pancreatic alpha-amylase inhibitor trestatin into bread on postprandial plasma glucose and insulin excursions was tested in healthy volunteers and non-insulin-dependent diabetic patients.
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2 |
1875725
|
Effects of age on diabetes- and insulin-induced changes in pancreatic levels of alpha-amylase and its mRNA.
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3 |
2143513
|
Effects of diabetes and insulin on alpha-amylase messenger RNA levels in rat parotid glands.
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4 |
2667315
|
Insulin and glycemic responses in healthy humans to native starches processed in different ways: correlation with in vitro alpha-amylase hydrolysis.
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5 |
3802496
|
Biological intra-individual variation in concentrations of 16 clinical biochemical analytes in serum was estimated for 27 patients with insulin-dependent diabetes mellitus (IDDM), and results were compared with those for apparently healthy individuals.
|
6 |
3802496
|
The ratio of the average intra-individual variation in IDDM patients to that in normal subjects exceeded 2.0 for Na+, K+, creatinine, and alpha-amylase; 1.50 to 2.0 for Cl-, total protein, albumin, cholesterol, and hemoglobin; and 1.2 to 1.5 for urea, uric acid, high-density-lipoprotein cholesterol, and aspartate aminotransferase.
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7 |
3802496
|
Average intra-individual variations were greater for women than for men for Na+, total protein, albumin, and hemoglobin.
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8 |
6376235
|
The effect of a new specific alpha-amylase inhibitor on post-prandial glucose and insulin excursions in normal subjects and Type 2 (non-insulin-dependent) diabetic patients.
|
9 |
6376235
|
Trestatin (Ro 9-0154), a new specific alpha-amylase inhibitor of microbial origin, was tested in six normal subjects and seven Type 2 (non-insulin-dependent) diabetic patients.
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10 |
6376235
|
The effect of a new specific alpha-amylase inhibitor on post-prandial glucose and insulin excursions in normal subjects and Type 2 (non-insulin-dependent) diabetic patients.
|
11 |
6376235
|
Trestatin (Ro 9-0154), a new specific alpha-amylase inhibitor of microbial origin, was tested in six normal subjects and seven Type 2 (non-insulin-dependent) diabetic patients.
|
12 |
6611154
|
However, there were no such differences in the levels of acid phosphatase or alpha-amylase.
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13 |
7955128
|
Glycogen synthase, glycogen phosphorylase and alpha-amylase activity in homogenates of islets of GK rats: comparison with hepatic and pancreatic extracts.
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14 |
7955128
|
Therefore, the activities of glycogen synthase, glycogen phosphorylase and alpha-amylase were measured in islets of control and GK rats.
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15 |
7955128
|
It is concluded that the diabetic syndrome in the GK rats does not involve any major anomaly of glycogen synthase and glycogen phosphorylase activity in the liver of these animals, as well as alpha-amylase, in pancreatic islets.
|
16 |
7955128
|
Glycogen synthase, glycogen phosphorylase and alpha-amylase activity in homogenates of islets of GK rats: comparison with hepatic and pancreatic extracts.
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17 |
7955128
|
Therefore, the activities of glycogen synthase, glycogen phosphorylase and alpha-amylase were measured in islets of control and GK rats.
|
18 |
7955128
|
It is concluded that the diabetic syndrome in the GK rats does not involve any major anomaly of glycogen synthase and glycogen phosphorylase activity in the liver of these animals, as well as alpha-amylase, in pancreatic islets.
|
19 |
7955128
|
Glycogen synthase, glycogen phosphorylase and alpha-amylase activity in homogenates of islets of GK rats: comparison with hepatic and pancreatic extracts.
|
20 |
7955128
|
Therefore, the activities of glycogen synthase, glycogen phosphorylase and alpha-amylase were measured in islets of control and GK rats.
|
21 |
7955128
|
It is concluded that the diabetic syndrome in the GK rats does not involve any major anomaly of glycogen synthase and glycogen phosphorylase activity in the liver of these animals, as well as alpha-amylase, in pancreatic islets.
|
22 |
8001624
|
The development of alpha-amylase and brush-border alpha-glucosidase inhibitors is reviewed.
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23 |
11193416
|
Twenty-one naturally occurring flavonoids were tested for inhibitory activities against alpha-glucosidase (EC 3.2.1.20) and alpha-amylase (EC 3.2.1.1).
|
24 |
11193416
|
Luteolin inhibited alpha-glucosidase by 36% at the concentration of 0.5 mg/ml and was stronger than acarbose, the most widely prescribed drug, in inhibitory potency, suggesting that it has the possibility to effectively suppress postprandial hyperglycemia in patients with non-insulin dependent diabetes mellitus.
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25 |
11427050
|
The nitrogen analogues 11 and 12 showed no significant inhibitory effect of either barley alpha-amylase (AMY1) or porcine pancreatic alpha-amylase (PPA) at concentrations of 5 mM.
|
26 |
11427050
|
In contrast, salacinol (7) inhibited AMY1 and PPA in the micromolar range, with K(i) values of 15 +/- 1 and 10 +/- 2 microM, respectively.
|
27 |
11427050
|
The nitrogen analogues 11 and 12 showed no significant inhibitory effect of either barley alpha-amylase (AMY1) or porcine pancreatic alpha-amylase (PPA) at concentrations of 5 mM.
|
28 |
11427050
|
In contrast, salacinol (7) inhibited AMY1 and PPA in the micromolar range, with K(i) values of 15 +/- 1 and 10 +/- 2 microM, respectively.
|
29 |
12656461
|
Total proteins, sugars and calcium were determined by colorimetric methods, and glucose, urea, alpha-amylase and acid phosphatase by enzymatic methods.
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30 |
15340182
|
The present study investigated the effects of Ginkgo biloba extract and its flavonoid fractions on alpha-amylase and alpha-glucosidase activity in vitro.
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31 |
15340182
|
Ginkgo biloba extracts and their flavonoid fraction significantly inhibited alpha-amylase and alpha-glucosidase activity in vitro.
|
32 |
15340182
|
The present study investigated the effects of Ginkgo biloba extract and its flavonoid fractions on alpha-amylase and alpha-glucosidase activity in vitro.
|
33 |
15340182
|
Ginkgo biloba extracts and their flavonoid fraction significantly inhibited alpha-amylase and alpha-glucosidase activity in vitro.
|
34 |
15618610
|
A hot water extract obtained by boiling adzuki beans (Vigna angularis) to produce bean paste for Japanese cake showed inhibitory activity against alpha-glucosidase, alpha-amylase, maltase, sucrase, and isomaltase after HP-20 column chromatography.
|
35 |
15618610
|
The active fraction showed potential hypoglycemic activity in both normal mice and streptozotocin (STZ)-induced diabetic rats after an oral administration of sucrose, but did not show any effect on the blood glucose concentration after glucose administration, suggesting that the active fraction suppressed the postprandial blood glucose level by inhibiting alpha-glucosidase and alpha-amylase, irrespective of the endogenous blood insulin level.
|
36 |
15618610
|
A hot water extract obtained by boiling adzuki beans (Vigna angularis) to produce bean paste for Japanese cake showed inhibitory activity against alpha-glucosidase, alpha-amylase, maltase, sucrase, and isomaltase after HP-20 column chromatography.
|
37 |
15618610
|
The active fraction showed potential hypoglycemic activity in both normal mice and streptozotocin (STZ)-induced diabetic rats after an oral administration of sucrose, but did not show any effect on the blood glucose concentration after glucose administration, suggesting that the active fraction suppressed the postprandial blood glucose level by inhibiting alpha-glucosidase and alpha-amylase, irrespective of the endogenous blood insulin level.
|
38 |
15927931
|
Key enzymes involved in the enzymatic breakdown of complex carbohydrates,pancreatic alpha-amylase and intestinal alpha-glucosidase, have been targeted as potential avenues for modulation of type 2 diabetes-associated post-prandial hyperglycemia through mild inhibition of their enzymatic activities so as to decrease meal-derived glucose absorption.
|
39 |
15927931
|
Water-soluble extracts of soybean optimized for phenolic content via sprouting or bioprocessing by dietary fungus (Rhizopus oligosporus, Lentinus edodes) were investigated for inhibitory activity against porcine pancreatic alpha-amylase (PPA), yeast alpha-glucosidase, and rabbit lung ACE in vitro.
|
40 |
15927931
|
Alpha-glucosidase and ACE activities were determined in the presence of each phenolic-optimized extract.
|
41 |
15927931
|
Key enzymes involved in the enzymatic breakdown of complex carbohydrates,pancreatic alpha-amylase and intestinal alpha-glucosidase, have been targeted as potential avenues for modulation of type 2 diabetes-associated post-prandial hyperglycemia through mild inhibition of their enzymatic activities so as to decrease meal-derived glucose absorption.
|
42 |
15927931
|
Water-soluble extracts of soybean optimized for phenolic content via sprouting or bioprocessing by dietary fungus (Rhizopus oligosporus, Lentinus edodes) were investigated for inhibitory activity against porcine pancreatic alpha-amylase (PPA), yeast alpha-glucosidase, and rabbit lung ACE in vitro.
|
43 |
15927931
|
Alpha-glucosidase and ACE activities were determined in the presence of each phenolic-optimized extract.
|
44 |
16500886
|
In the current study, we screened 7 clonal lines from single seed phenotypes of Lamiaceae family for the inhibition of alpha-amylase, alpha-glucosidase and angiotensin converting enzyme (ACE) inhibitory activity.
|
45 |
16837437
|
In the current study, we investigated 2 species of the genus Rhodiola for the inhibition of alpha-amylase,alpha-glucosidase and angiotensin converting enzyme (ACE) inhibitory activity.
|
46 |
16837437
|
Tyrosol had strong alpha-glucosidase inhibitory activity (IC50, 70.8 microg total phenolic/ml) but did not have any inhibitory effect on the alpha-amylase activity.
|
47 |
16837437
|
In the current study, we investigated 2 species of the genus Rhodiola for the inhibition of alpha-amylase,alpha-glucosidase and angiotensin converting enzyme (ACE) inhibitory activity.
|
48 |
16837437
|
Tyrosol had strong alpha-glucosidase inhibitory activity (IC50, 70.8 microg total phenolic/ml) but did not have any inhibitory effect on the alpha-amylase activity.
|
49 |
16837438
|
Water soluble cranberry-based phytochemical combinations with oregano, rosemary, and Rhodiola rosea were evaluated for total phenolic content, related antioxidant activity and inhibition of diabetes management-related alpha -glucosidase, pancreatic alpha-amylase inhibition, and hypertension-related ACE-I inhibitory activities.
|
50 |
16837438
|
The analysis of alpha -glucosidase,alpha -amylase, and ACE-I inhibitory activities suggested that inhibition depend on the phenolic profile of each unique extract and by bringing together synergistic combinations to cranberry, health beneficial functionality was enhanced.
|
51 |
16837438
|
This enhanced functionality in terms of high alpha -glucosidase and alpha -amylase inhibitory activities indicate the potential for diabetes management, and high ACE-I inhibitory activity indicates the potential for hypertension management.
|
52 |
16837438
|
Water soluble cranberry-based phytochemical combinations with oregano, rosemary, and Rhodiola rosea were evaluated for total phenolic content, related antioxidant activity and inhibition of diabetes management-related alpha -glucosidase, pancreatic alpha-amylase inhibition, and hypertension-related ACE-I inhibitory activities.
|
53 |
16837438
|
The analysis of alpha -glucosidase,alpha -amylase, and ACE-I inhibitory activities suggested that inhibition depend on the phenolic profile of each unique extract and by bringing together synergistic combinations to cranberry, health beneficial functionality was enhanced.
|
54 |
16837438
|
This enhanced functionality in terms of high alpha -glucosidase and alpha -amylase inhibitory activities indicate the potential for diabetes management, and high ACE-I inhibitory activity indicates the potential for hypertension management.
|
55 |
16837438
|
Water soluble cranberry-based phytochemical combinations with oregano, rosemary, and Rhodiola rosea were evaluated for total phenolic content, related antioxidant activity and inhibition of diabetes management-related alpha -glucosidase, pancreatic alpha-amylase inhibition, and hypertension-related ACE-I inhibitory activities.
|
56 |
16837438
|
The analysis of alpha -glucosidase,alpha -amylase, and ACE-I inhibitory activities suggested that inhibition depend on the phenolic profile of each unique extract and by bringing together synergistic combinations to cranberry, health beneficial functionality was enhanced.
|
57 |
16837438
|
This enhanced functionality in terms of high alpha -glucosidase and alpha -amylase inhibitory activities indicate the potential for diabetes management, and high ACE-I inhibitory activity indicates the potential for hypertension management.
|
58 |
17244479
|
A comparison of ghrelin, glucose, alpha-amylase and protein levels in saliva from diabetics.
|
59 |
17628531
|
Following the intake of CCT diet for 14 consecutive days a decrease in the serum levels of insulin, both the thyroid hormones, triiodothyronine (T(3)) and thyroxine (T(4)); hepatic glycogen content, hepatic type-1 iodothyronine 5'-mono-deiodinase (5'D) and serum alpha-amylase activities were observed, while there was an increase in the levels of serum glucose and nitrite and in lipid peroxidation of heart, liver and kidney tissues as well as in serum.
|
60 |
17628531
|
However, simultaneous administration of L-thyroxine (500 microg/kg/day, s.c.) to CCT-diet fed animals resulted in the amelioration of all the aforesaid adverse changes including that of serum glucose, insulin, alpha-amylase, hepatic glycogen content and nitrite levels, suggesting the involvement of thyroid hormones in the progression of CCT-diet induced diabetes mellitus.
|
61 |
17628531
|
Following the intake of CCT diet for 14 consecutive days a decrease in the serum levels of insulin, both the thyroid hormones, triiodothyronine (T(3)) and thyroxine (T(4)); hepatic glycogen content, hepatic type-1 iodothyronine 5'-mono-deiodinase (5'D) and serum alpha-amylase activities were observed, while there was an increase in the levels of serum glucose and nitrite and in lipid peroxidation of heart, liver and kidney tissues as well as in serum.
|
62 |
17628531
|
However, simultaneous administration of L-thyroxine (500 microg/kg/day, s.c.) to CCT-diet fed animals resulted in the amelioration of all the aforesaid adverse changes including that of serum glucose, insulin, alpha-amylase, hepatic glycogen content and nitrite levels, suggesting the involvement of thyroid hormones in the progression of CCT-diet induced diabetes mellitus.
|
63 |
18511986
|
In vitro alpha-glucosidase and alpha-amylase enzyme inhibitory effects of Andrographis paniculata extract and andrographolide.
|
64 |
18511986
|
The goal of the present study was to provide in vitro evidence for potential inhibition of alpha-glucosidase and alpha-amylase enzymes, followed by a confirmatory in vivo study on rats to generate a stronger biochemical rationale for further studies on the ethanolic extract of Andrographis paniculata and andrographolide.
|
65 |
18511986
|
The extract showed appreciable alpha-glucosidase inhibitory effect in a concentration-dependent manner (IC(50)=17.2+/-0.15 mg/ml) and a weak alpha-amylase inhibitory activity (IC(50)=50.9+/-0.17 mg/ml).
|
66 |
18511986
|
Andrographolide demonstrated a similar (IC(50)=11.0+/-0.28 mg/ml) alpha-glucosidase and alpha-amylase inhibitory activity (IC(50)=11.3+/-0.29 mg/ml).
|
67 |
18511986
|
In vitro alpha-glucosidase and alpha-amylase enzyme inhibitory effects of Andrographis paniculata extract and andrographolide.
|
68 |
18511986
|
The goal of the present study was to provide in vitro evidence for potential inhibition of alpha-glucosidase and alpha-amylase enzymes, followed by a confirmatory in vivo study on rats to generate a stronger biochemical rationale for further studies on the ethanolic extract of Andrographis paniculata and andrographolide.
|
69 |
18511986
|
The extract showed appreciable alpha-glucosidase inhibitory effect in a concentration-dependent manner (IC(50)=17.2+/-0.15 mg/ml) and a weak alpha-amylase inhibitory activity (IC(50)=50.9+/-0.17 mg/ml).
|
70 |
18511986
|
Andrographolide demonstrated a similar (IC(50)=11.0+/-0.28 mg/ml) alpha-glucosidase and alpha-amylase inhibitory activity (IC(50)=11.3+/-0.29 mg/ml).
|
71 |
18511986
|
In vitro alpha-glucosidase and alpha-amylase enzyme inhibitory effects of Andrographis paniculata extract and andrographolide.
|
72 |
18511986
|
The goal of the present study was to provide in vitro evidence for potential inhibition of alpha-glucosidase and alpha-amylase enzymes, followed by a confirmatory in vivo study on rats to generate a stronger biochemical rationale for further studies on the ethanolic extract of Andrographis paniculata and andrographolide.
|
73 |
18511986
|
The extract showed appreciable alpha-glucosidase inhibitory effect in a concentration-dependent manner (IC(50)=17.2+/-0.15 mg/ml) and a weak alpha-amylase inhibitory activity (IC(50)=50.9+/-0.17 mg/ml).
|
74 |
18511986
|
Andrographolide demonstrated a similar (IC(50)=11.0+/-0.28 mg/ml) alpha-glucosidase and alpha-amylase inhibitory activity (IC(50)=11.3+/-0.29 mg/ml).
|
75 |
18511986
|
In vitro alpha-glucosidase and alpha-amylase enzyme inhibitory effects of Andrographis paniculata extract and andrographolide.
|
76 |
18511986
|
The goal of the present study was to provide in vitro evidence for potential inhibition of alpha-glucosidase and alpha-amylase enzymes, followed by a confirmatory in vivo study on rats to generate a stronger biochemical rationale for further studies on the ethanolic extract of Andrographis paniculata and andrographolide.
|
77 |
18511986
|
The extract showed appreciable alpha-glucosidase inhibitory effect in a concentration-dependent manner (IC(50)=17.2+/-0.15 mg/ml) and a weak alpha-amylase inhibitory activity (IC(50)=50.9+/-0.17 mg/ml).
|
78 |
18511986
|
Andrographolide demonstrated a similar (IC(50)=11.0+/-0.28 mg/ml) alpha-glucosidase and alpha-amylase inhibitory activity (IC(50)=11.3+/-0.29 mg/ml).
|
79 |
18553919
|
Both inhibited rat intestine alpha-glucosidase competitively but displayed a mixed-type inhibition mode against human pancreatic alpha-amylase.
|
80 |
18553919
|
In contrast, the alpha-acarviosinyl-(1-->9)-3-alpha-D-glucopyranosylpropen exhibited a 3.0-fold improved inhibition potency against rat intestine alpha-glucosidase with 0.3-fold inhibition potency against human pancreatic alpha-amylase relative to acarbose.
|
81 |
18553919
|
In conclusion, alpha-acarviosinyl-(1-->9)-3-alpha-D-glucopyranosylpropen is a novel alpha-glucosidase-selective inhibitor with 10-fold enhanced selectivity toward alpha-glucosidase over alpha-amylase relative to acarbose, and it could be applied as a potent hypoglycemic agent.
|
82 |
18553919
|
Both inhibited rat intestine alpha-glucosidase competitively but displayed a mixed-type inhibition mode against human pancreatic alpha-amylase.
|
83 |
18553919
|
In contrast, the alpha-acarviosinyl-(1-->9)-3-alpha-D-glucopyranosylpropen exhibited a 3.0-fold improved inhibition potency against rat intestine alpha-glucosidase with 0.3-fold inhibition potency against human pancreatic alpha-amylase relative to acarbose.
|
84 |
18553919
|
In conclusion, alpha-acarviosinyl-(1-->9)-3-alpha-D-glucopyranosylpropen is a novel alpha-glucosidase-selective inhibitor with 10-fold enhanced selectivity toward alpha-glucosidase over alpha-amylase relative to acarbose, and it could be applied as a potent hypoglycemic agent.
|
85 |
18553919
|
Both inhibited rat intestine alpha-glucosidase competitively but displayed a mixed-type inhibition mode against human pancreatic alpha-amylase.
|
86 |
18553919
|
In contrast, the alpha-acarviosinyl-(1-->9)-3-alpha-D-glucopyranosylpropen exhibited a 3.0-fold improved inhibition potency against rat intestine alpha-glucosidase with 0.3-fold inhibition potency against human pancreatic alpha-amylase relative to acarbose.
|
87 |
18553919
|
In conclusion, alpha-acarviosinyl-(1-->9)-3-alpha-D-glucopyranosylpropen is a novel alpha-glucosidase-selective inhibitor with 10-fold enhanced selectivity toward alpha-glucosidase over alpha-amylase relative to acarbose, and it could be applied as a potent hypoglycemic agent.
|
88 |
18598178
|
Brown sugar from Peru and Mauritius (dark muscovado) had the highest total phenolic content and 1,1-diphenyl-2-picrylhydrazyl radical scavenging activity, which correlated with a moderate inhibition of yeast alpha-glucosidase without showing a significant effect on porcine pancreatic alpha-amylase activity.
|
89 |
18598178
|
Date sugar exhibited high alpha-glucosidase, alpha-amylase, and ACE inhibitory activities that correlated with high total phenolic content and antioxidant activity.
|
90 |
18598178
|
Neither phenolic compounds or antioxidant activity was detected in corn syrups, indicating that nonphenolic factors may be involved in their significant ability to inhibit alpha-glucosidase, alpha-amylase, and ACE.
|
91 |
18598178
|
Brown sugar from Peru and Mauritius (dark muscovado) had the highest total phenolic content and 1,1-diphenyl-2-picrylhydrazyl radical scavenging activity, which correlated with a moderate inhibition of yeast alpha-glucosidase without showing a significant effect on porcine pancreatic alpha-amylase activity.
|
92 |
18598178
|
Date sugar exhibited high alpha-glucosidase, alpha-amylase, and ACE inhibitory activities that correlated with high total phenolic content and antioxidant activity.
|
93 |
18598178
|
Neither phenolic compounds or antioxidant activity was detected in corn syrups, indicating that nonphenolic factors may be involved in their significant ability to inhibit alpha-glucosidase, alpha-amylase, and ACE.
|
94 |
18598178
|
Brown sugar from Peru and Mauritius (dark muscovado) had the highest total phenolic content and 1,1-diphenyl-2-picrylhydrazyl radical scavenging activity, which correlated with a moderate inhibition of yeast alpha-glucosidase without showing a significant effect on porcine pancreatic alpha-amylase activity.
|
95 |
18598178
|
Date sugar exhibited high alpha-glucosidase, alpha-amylase, and ACE inhibitory activities that correlated with high total phenolic content and antioxidant activity.
|
96 |
18598178
|
Neither phenolic compounds or antioxidant activity was detected in corn syrups, indicating that nonphenolic factors may be involved in their significant ability to inhibit alpha-glucosidase, alpha-amylase, and ACE.
|
97 |
18806305
|
While a single dose of alloxan (120 mg/kg) increased the serum levels of glucose and alpha-amylase activity, rate of water consumption and lipid peroxidation (LPO) in hepatic, cardiac and renal tissues with a parallel decrease in serum insulin level, administration of 25 mg/kg of CS or 200 mg/kg of PG was found to normalize all the adverse changes induced by alloxan, revealing the antidiabetic and anti peroxidative potential of test fruit peel extracts.
|
98 |
19001775
|
Chestnut astringent skin (CAS) extract inhibited pancreatic alpha-amylase and intestinal alpha-glucosidase in a concentration-dependent manner with the 50% inhibition concentration (IC50) for amylase, maltase and sucrase being 7.5, 650 and 390 microg/mL, respectively.
|
99 |
19457656
|
Anti-diabetes-relevant alpha-amylase inhibition percent (AIP) and alpha-glucosidase inhibition percent (GIP) were high in the cotyledons and decreased following elicitation and sprouting.
|
100 |
19482018
|
Diphlorethohydroxycarmalol isolated from Ishige okamurae, a brown algae, a potent alpha-glucosidase and alpha-amylase inhibitor, alleviates postprandial hyperglycemia in diabetic mice.
|
101 |
19482018
|
This study was designed to investigate whether diphlorethohydroxycarmalol (DPHC) may inhibit alpha-glucosidase and alpha-amylase activities, and alleviate postprandial hyperglycemia in streptozotocin-induced diabetic mice.
|
102 |
19482018
|
DPHC isolated from Ishige okamurae, a brown algae, evidenced prominent inhibitory effect against alpha-glucosidase and alpha-amylase.
|
103 |
19482018
|
The IC(50) values of DPHC against alpha-glucosidase and alpha-amylase were 0.16 and 0.53 mM, respectively, which evidenced the higher activities than that of acarbose.
|
104 |
19482018
|
Therefore, these result indicated that DPHC might be a potent inhibitor for alpha-glucosidase and alpha-amylase.
|
105 |
19482018
|
Diphlorethohydroxycarmalol isolated from Ishige okamurae, a brown algae, a potent alpha-glucosidase and alpha-amylase inhibitor, alleviates postprandial hyperglycemia in diabetic mice.
|
106 |
19482018
|
This study was designed to investigate whether diphlorethohydroxycarmalol (DPHC) may inhibit alpha-glucosidase and alpha-amylase activities, and alleviate postprandial hyperglycemia in streptozotocin-induced diabetic mice.
|
107 |
19482018
|
DPHC isolated from Ishige okamurae, a brown algae, evidenced prominent inhibitory effect against alpha-glucosidase and alpha-amylase.
|
108 |
19482018
|
The IC(50) values of DPHC against alpha-glucosidase and alpha-amylase were 0.16 and 0.53 mM, respectively, which evidenced the higher activities than that of acarbose.
|
109 |
19482018
|
Therefore, these result indicated that DPHC might be a potent inhibitor for alpha-glucosidase and alpha-amylase.
|
110 |
19482018
|
Diphlorethohydroxycarmalol isolated from Ishige okamurae, a brown algae, a potent alpha-glucosidase and alpha-amylase inhibitor, alleviates postprandial hyperglycemia in diabetic mice.
|
111 |
19482018
|
This study was designed to investigate whether diphlorethohydroxycarmalol (DPHC) may inhibit alpha-glucosidase and alpha-amylase activities, and alleviate postprandial hyperglycemia in streptozotocin-induced diabetic mice.
|
112 |
19482018
|
DPHC isolated from Ishige okamurae, a brown algae, evidenced prominent inhibitory effect against alpha-glucosidase and alpha-amylase.
|
113 |
19482018
|
The IC(50) values of DPHC against alpha-glucosidase and alpha-amylase were 0.16 and 0.53 mM, respectively, which evidenced the higher activities than that of acarbose.
|
114 |
19482018
|
Therefore, these result indicated that DPHC might be a potent inhibitor for alpha-glucosidase and alpha-amylase.
|
115 |
19482018
|
Diphlorethohydroxycarmalol isolated from Ishige okamurae, a brown algae, a potent alpha-glucosidase and alpha-amylase inhibitor, alleviates postprandial hyperglycemia in diabetic mice.
|
116 |
19482018
|
This study was designed to investigate whether diphlorethohydroxycarmalol (DPHC) may inhibit alpha-glucosidase and alpha-amylase activities, and alleviate postprandial hyperglycemia in streptozotocin-induced diabetic mice.
|
117 |
19482018
|
DPHC isolated from Ishige okamurae, a brown algae, evidenced prominent inhibitory effect against alpha-glucosidase and alpha-amylase.
|
118 |
19482018
|
The IC(50) values of DPHC against alpha-glucosidase and alpha-amylase were 0.16 and 0.53 mM, respectively, which evidenced the higher activities than that of acarbose.
|
119 |
19482018
|
Therefore, these result indicated that DPHC might be a potent inhibitor for alpha-glucosidase and alpha-amylase.
|
120 |
19482018
|
Diphlorethohydroxycarmalol isolated from Ishige okamurae, a brown algae, a potent alpha-glucosidase and alpha-amylase inhibitor, alleviates postprandial hyperglycemia in diabetic mice.
|
121 |
19482018
|
This study was designed to investigate whether diphlorethohydroxycarmalol (DPHC) may inhibit alpha-glucosidase and alpha-amylase activities, and alleviate postprandial hyperglycemia in streptozotocin-induced diabetic mice.
|
122 |
19482018
|
DPHC isolated from Ishige okamurae, a brown algae, evidenced prominent inhibitory effect against alpha-glucosidase and alpha-amylase.
|
123 |
19482018
|
The IC(50) values of DPHC against alpha-glucosidase and alpha-amylase were 0.16 and 0.53 mM, respectively, which evidenced the higher activities than that of acarbose.
|
124 |
19482018
|
Therefore, these result indicated that DPHC might be a potent inhibitor for alpha-glucosidase and alpha-amylase.
|
125 |
19665890
|
Water and 12% ethanol extracts were analyzed for total phenolics content, antioxidant activity, phenolic profile, and the potential in vitro inhibitory effects on alpha-amylase, alpha-glucosidase, and Angiotensin I-Converting Enzyme (ACE) enzymes related to the management of diabetes and hypertension.
|
126 |
19695871
|
In vitro inhibition of alpha-amylase, alpha-glucosidase, and angiotensin-1-converting enzyme (ACE) activity was evaluated using fruit extracts and correlated to phenolic content and antioxidant activity.
|
127 |
19695871
|
Strawberry cultivars with combined inhibitory potential against alpha-glucosidase and ACE and with moderate or low alpha-amylase inhibitory potential could be targeted for potential management of hyperglycemia-linked type 2 diabetes and related complication of hypertension.
|
128 |
19695871
|
In vitro inhibition of alpha-amylase, alpha-glucosidase, and angiotensin-1-converting enzyme (ACE) activity was evaluated using fruit extracts and correlated to phenolic content and antioxidant activity.
|
129 |
19695871
|
Strawberry cultivars with combined inhibitory potential against alpha-glucosidase and ACE and with moderate or low alpha-amylase inhibitory potential could be targeted for potential management of hyperglycemia-linked type 2 diabetes and related complication of hypertension.
|
130 |
19772492
|
Inhibition of alpha-glucosidase and alpha-amylase delays the digestion of starch and disaccharides to absorbable monosaccharides, resulting in a reduction of postprandial hyperglycemia.
|
131 |
19772492
|
We investigated the inhibitory activity of cinnamic acid derivatives against rat intestinal alpha-glucosidase and porcine pancreatic alpha-amylase in vitro.
|
132 |
19772492
|
Inhibition of alpha-glucosidase and alpha-amylase delays the digestion of starch and disaccharides to absorbable monosaccharides, resulting in a reduction of postprandial hyperglycemia.
|
133 |
19772492
|
We investigated the inhibitory activity of cinnamic acid derivatives against rat intestinal alpha-glucosidase and porcine pancreatic alpha-amylase in vitro.
|
134 |
20109131
|
Evaluation of alpha-glucosidase, alpha-amylase and protein glycation inhibitory activities of edible plants.
|
135 |
20109131
|
The present study was to investigate in vitro alpha-glucosidase, pancreatic alpha-amylase and protein glycation inhibitory activities of nine edible plants.
|
136 |
20109131
|
Evaluation of alpha-glucosidase, alpha-amylase and protein glycation inhibitory activities of edible plants.
|
137 |
20109131
|
The present study was to investigate in vitro alpha-glucosidase, pancreatic alpha-amylase and protein glycation inhibitory activities of nine edible plants.
|
138 |
20347903
|
Amylin (Amy) receptors are complexes of the calcitonin receptor with receptor activity-modifying proteins.
|
139 |
20347903
|
RAMP1 with the calcitonin receptor forms the AMY(1) receptor; the insert negative isoform of the calcitonin receptor in this complex makes the AMY(1(a)) receptor.
|
140 |
20347903
|
This receptor has high affinity for Amy and the related peptide calcitonin gene-related peptide (CGRP).
|
141 |
20347903
|
It has been suggested that the peptides bind in a pocket formed between the long N-termini of the calcitonin receptor and RAMP1, although very few residues in either component have been assigned specific roles.
|
142 |
20347903
|
Here, Arg67, Asp71, Glu78 and Trp84 were individually mutated to alanine and the function of mutant AMY(1(a)) receptors was determined using a cAMP assay.
|
143 |
20347903
|
Mutation of Arg67, Asp71 and Glu78 had no significant effect on Amy or CGRP potency, cell surface or total expression.
|
144 |
20347903
|
The data reveal the importance of Trp84 in the AMY(1(a)) receptor.
|
145 |
20470247
|
Natural products as alpha-amylase and alpha-glucosidase inhibitors and their hypoglycaemic potential in the treatment of diabetes: an update.
|
146 |
20470247
|
The inhibition of alpha-glucosidase and alpha-amylase, enzymes involved in the digestion of carbohydrates, can significantly reduce the post-prandial increase of blood glucose and therefore can be an important strategy in the management of blood glucose level in type 2 diabetic and borderline patients.
|
147 |
20470247
|
Therefore, natural alpha-glucosidase and alpha-amylase inhibitors from plant sources offer an attractive strategy for the control of hyperglycaemia.
|
148 |
20470247
|
Natural products as alpha-amylase and alpha-glucosidase inhibitors and their hypoglycaemic potential in the treatment of diabetes: an update.
|
149 |
20470247
|
The inhibition of alpha-glucosidase and alpha-amylase, enzymes involved in the digestion of carbohydrates, can significantly reduce the post-prandial increase of blood glucose and therefore can be an important strategy in the management of blood glucose level in type 2 diabetic and borderline patients.
|
150 |
20470247
|
Therefore, natural alpha-glucosidase and alpha-amylase inhibitors from plant sources offer an attractive strategy for the control of hyperglycaemia.
|
151 |
20470247
|
Natural products as alpha-amylase and alpha-glucosidase inhibitors and their hypoglycaemic potential in the treatment of diabetes: an update.
|
152 |
20470247
|
The inhibition of alpha-glucosidase and alpha-amylase, enzymes involved in the digestion of carbohydrates, can significantly reduce the post-prandial increase of blood glucose and therefore can be an important strategy in the management of blood glucose level in type 2 diabetic and borderline patients.
|
153 |
20470247
|
Therefore, natural alpha-glucosidase and alpha-amylase inhibitors from plant sources offer an attractive strategy for the control of hyperglycaemia.
|
154 |
20600532
|
Dieckol isolated from Ecklonia cava inhibits alpha-glucosidase and alpha-amylase in vitro and alleviates postprandial hyperglycemia in streptozotocin-induced diabetic mice.
|
155 |
20600532
|
Dieckol isolated from Ecklonia cava, brown algae, evidenced prominent inhibitory effect against alpha-glucosidase and alpha-amylase.
|
156 |
20600532
|
The IC(50) values of dieckol against alpha-glucosidase and alpha-amylase were 0.24 and 0.66 mM, respectively, which evidenced the higher activities than that of acarbose.
|
157 |
20600532
|
Dieckol isolated from Ecklonia cava inhibits alpha-glucosidase and alpha-amylase in vitro and alleviates postprandial hyperglycemia in streptozotocin-induced diabetic mice.
|
158 |
20600532
|
Dieckol isolated from Ecklonia cava, brown algae, evidenced prominent inhibitory effect against alpha-glucosidase and alpha-amylase.
|
159 |
20600532
|
The IC(50) values of dieckol against alpha-glucosidase and alpha-amylase were 0.24 and 0.66 mM, respectively, which evidenced the higher activities than that of acarbose.
|
160 |
20600532
|
Dieckol isolated from Ecklonia cava inhibits alpha-glucosidase and alpha-amylase in vitro and alleviates postprandial hyperglycemia in streptozotocin-induced diabetic mice.
|
161 |
20600532
|
Dieckol isolated from Ecklonia cava, brown algae, evidenced prominent inhibitory effect against alpha-glucosidase and alpha-amylase.
|
162 |
20600532
|
The IC(50) values of dieckol against alpha-glucosidase and alpha-amylase were 0.24 and 0.66 mM, respectively, which evidenced the higher activities than that of acarbose.
|
163 |
22224265
|
South African plants namely Terminalia sericea, Euclea natalensis, Warbugia salutaris, Aloe ferox, Artemisia afra, Sclerocarya birrea, Spirostachys africana and Psidium guajava were investigated for their in vitro alpha-glucosidase and alpha-amylase properties, and antioxidant activities.
|
164 |
22224265
|
Terminalia sericea stem bark extract showed the best results against alpha-glucosidase and alpha-amylase enzymes.
|
165 |
22224265
|
This study is the first to report alpha-glucosidase and alpha-amylase activity of M1, M2, 2 and 4 isolated from T. sericea, which validated the traditional use of the bark of T. sericea for diabetes in South Africa.
|
166 |
22224265
|
South African plants namely Terminalia sericea, Euclea natalensis, Warbugia salutaris, Aloe ferox, Artemisia afra, Sclerocarya birrea, Spirostachys africana and Psidium guajava were investigated for their in vitro alpha-glucosidase and alpha-amylase properties, and antioxidant activities.
|
167 |
22224265
|
Terminalia sericea stem bark extract showed the best results against alpha-glucosidase and alpha-amylase enzymes.
|
168 |
22224265
|
This study is the first to report alpha-glucosidase and alpha-amylase activity of M1, M2, 2 and 4 isolated from T. sericea, which validated the traditional use of the bark of T. sericea for diabetes in South Africa.
|
169 |
22224265
|
South African plants namely Terminalia sericea, Euclea natalensis, Warbugia salutaris, Aloe ferox, Artemisia afra, Sclerocarya birrea, Spirostachys africana and Psidium guajava were investigated for their in vitro alpha-glucosidase and alpha-amylase properties, and antioxidant activities.
|
170 |
22224265
|
Terminalia sericea stem bark extract showed the best results against alpha-glucosidase and alpha-amylase enzymes.
|
171 |
22224265
|
This study is the first to report alpha-glucosidase and alpha-amylase activity of M1, M2, 2 and 4 isolated from T. sericea, which validated the traditional use of the bark of T. sericea for diabetes in South Africa.
|
172 |
22492122
|
The samples were analyzed for plasma glucose and insulin concentrations as well as diploid AMY1 gene copy number.
|
173 |
22492122
|
HA individuals had significantly more AMY1 gene copies within their genomes than did the LA individuals.
|
174 |
22492122
|
The samples were analyzed for plasma glucose and insulin concentrations as well as diploid AMY1 gene copy number.
|
175 |
22492122
|
HA individuals had significantly more AMY1 gene copies within their genomes than did the LA individuals.
|
176 |
22965187
|
The α-amylase genes are located in a cluster on the chromosome that includes salivary amylase genes (AMY1), two pancreatic α-amylase genes (AMY2A and AMY2B) and a related pseudogene.
|
177 |
22965187
|
The AMY1 genes show extensive copy number variation which is directly proportional to the salivary α-amylase content in saliva.
|
178 |
22965187
|
It has been shown that the average copy number of AMY1 gene is higher in populations that evolved under high-starch diets versus low-starch diets, reflecting an intense positive selection imposed by diet on amylase copy number during evolution.
|
179 |
22965187
|
In this context, a number of different aspects can be considered in evaluating the possible impact of copy number variation of the AMY1 gene on nutrition research, such as issues related to human diet gene evolution, action on starch digestion, effect on glycemic response after starch consumption, modulation of the action of α-amylases inhibitors, effect on taste perception and satiety, influence on psychosocial stress and relation to oral health.
|
180 |
22965187
|
The α-amylase genes are located in a cluster on the chromosome that includes salivary amylase genes (AMY1), two pancreatic α-amylase genes (AMY2A and AMY2B) and a related pseudogene.
|
181 |
22965187
|
The AMY1 genes show extensive copy number variation which is directly proportional to the salivary α-amylase content in saliva.
|
182 |
22965187
|
It has been shown that the average copy number of AMY1 gene is higher in populations that evolved under high-starch diets versus low-starch diets, reflecting an intense positive selection imposed by diet on amylase copy number during evolution.
|
183 |
22965187
|
In this context, a number of different aspects can be considered in evaluating the possible impact of copy number variation of the AMY1 gene on nutrition research, such as issues related to human diet gene evolution, action on starch digestion, effect on glycemic response after starch consumption, modulation of the action of α-amylases inhibitors, effect on taste perception and satiety, influence on psychosocial stress and relation to oral health.
|
184 |
22965187
|
The α-amylase genes are located in a cluster on the chromosome that includes salivary amylase genes (AMY1), two pancreatic α-amylase genes (AMY2A and AMY2B) and a related pseudogene.
|
185 |
22965187
|
The AMY1 genes show extensive copy number variation which is directly proportional to the salivary α-amylase content in saliva.
|
186 |
22965187
|
It has been shown that the average copy number of AMY1 gene is higher in populations that evolved under high-starch diets versus low-starch diets, reflecting an intense positive selection imposed by diet on amylase copy number during evolution.
|
187 |
22965187
|
In this context, a number of different aspects can be considered in evaluating the possible impact of copy number variation of the AMY1 gene on nutrition research, such as issues related to human diet gene evolution, action on starch digestion, effect on glycemic response after starch consumption, modulation of the action of α-amylases inhibitors, effect on taste perception and satiety, influence on psychosocial stress and relation to oral health.
|
188 |
22965187
|
The α-amylase genes are located in a cluster on the chromosome that includes salivary amylase genes (AMY1), two pancreatic α-amylase genes (AMY2A and AMY2B) and a related pseudogene.
|
189 |
22965187
|
The AMY1 genes show extensive copy number variation which is directly proportional to the salivary α-amylase content in saliva.
|
190 |
22965187
|
It has been shown that the average copy number of AMY1 gene is higher in populations that evolved under high-starch diets versus low-starch diets, reflecting an intense positive selection imposed by diet on amylase copy number during evolution.
|
191 |
22965187
|
In this context, a number of different aspects can be considered in evaluating the possible impact of copy number variation of the AMY1 gene on nutrition research, such as issues related to human diet gene evolution, action on starch digestion, effect on glycemic response after starch consumption, modulation of the action of α-amylases inhibitors, effect on taste perception and satiety, influence on psychosocial stress and relation to oral health.
|
192 |
23700798
|
alpha-Glucosidase and alpha-amylase inhibitory activities of saponins from traditional Chinese medicines in the treatment of diabetes mellitus.
|
193 |
23700798
|
Extracts of eleven traditional Chinese medicines (TCM) with a reputation of usefulness in treating diabetes mellitus were examined for alpha-glucosidase and alpha-amylase inhibitory activities in vitro.
|
194 |
23700798
|
To identify which constituents were responsible for the activities, thirteen triterpenoid saponins were isolated from EAT and examined for their inhibitory effects against alpha-glucosidase and alpha-amylase.
|
195 |
23700798
|
The results revealed that saponins 2, 3, 4 (IC50: 0.83 +/- 0.05 microM for BSG and IC50: 0.72 +/- 0.03 microM for SCG), 5, 6, 7, 9, 10, 11 and 12 (IC50: 1.07 +/- 0.04 micro.M for BSG and IC50: 0.93 +/- 0.05 micro.M for SCG) showed alpha-glucosidase inhibitory activities, while 2, 3, 4 (IC50: 0.93 +/- 0.04 micro.M for PPA), 5, 6, 7, 9, 10, 11 and 12 (IC50: 1.02 +/- 0.03 micro.M for PPA) possessed significant alpha-amylase inhibitory activities.
|
196 |
23700798
|
It is suggested that the glucuronic acid unit at C-3 of the aglycone is the imperative functional group of the antidiabetic activities, and two characteristic structural features are responsible for the remarkable alpha-glucosidase and alpha-amylase inhibitory activities.
|
197 |
23700798
|
alpha-Glucosidase and alpha-amylase inhibitory activities of saponins from traditional Chinese medicines in the treatment of diabetes mellitus.
|
198 |
23700798
|
Extracts of eleven traditional Chinese medicines (TCM) with a reputation of usefulness in treating diabetes mellitus were examined for alpha-glucosidase and alpha-amylase inhibitory activities in vitro.
|
199 |
23700798
|
To identify which constituents were responsible for the activities, thirteen triterpenoid saponins were isolated from EAT and examined for their inhibitory effects against alpha-glucosidase and alpha-amylase.
|
200 |
23700798
|
The results revealed that saponins 2, 3, 4 (IC50: 0.83 +/- 0.05 microM for BSG and IC50: 0.72 +/- 0.03 microM for SCG), 5, 6, 7, 9, 10, 11 and 12 (IC50: 1.07 +/- 0.04 micro.M for BSG and IC50: 0.93 +/- 0.05 micro.M for SCG) showed alpha-glucosidase inhibitory activities, while 2, 3, 4 (IC50: 0.93 +/- 0.04 micro.M for PPA), 5, 6, 7, 9, 10, 11 and 12 (IC50: 1.02 +/- 0.03 micro.M for PPA) possessed significant alpha-amylase inhibitory activities.
|
201 |
23700798
|
It is suggested that the glucuronic acid unit at C-3 of the aglycone is the imperative functional group of the antidiabetic activities, and two characteristic structural features are responsible for the remarkable alpha-glucosidase and alpha-amylase inhibitory activities.
|
202 |
23700798
|
alpha-Glucosidase and alpha-amylase inhibitory activities of saponins from traditional Chinese medicines in the treatment of diabetes mellitus.
|
203 |
23700798
|
Extracts of eleven traditional Chinese medicines (TCM) with a reputation of usefulness in treating diabetes mellitus were examined for alpha-glucosidase and alpha-amylase inhibitory activities in vitro.
|
204 |
23700798
|
To identify which constituents were responsible for the activities, thirteen triterpenoid saponins were isolated from EAT and examined for their inhibitory effects against alpha-glucosidase and alpha-amylase.
|
205 |
23700798
|
The results revealed that saponins 2, 3, 4 (IC50: 0.83 +/- 0.05 microM for BSG and IC50: 0.72 +/- 0.03 microM for SCG), 5, 6, 7, 9, 10, 11 and 12 (IC50: 1.07 +/- 0.04 micro.M for BSG and IC50: 0.93 +/- 0.05 micro.M for SCG) showed alpha-glucosidase inhibitory activities, while 2, 3, 4 (IC50: 0.93 +/- 0.04 micro.M for PPA), 5, 6, 7, 9, 10, 11 and 12 (IC50: 1.02 +/- 0.03 micro.M for PPA) possessed significant alpha-amylase inhibitory activities.
|
206 |
23700798
|
It is suggested that the glucuronic acid unit at C-3 of the aglycone is the imperative functional group of the antidiabetic activities, and two characteristic structural features are responsible for the remarkable alpha-glucosidase and alpha-amylase inhibitory activities.
|
207 |
23700798
|
alpha-Glucosidase and alpha-amylase inhibitory activities of saponins from traditional Chinese medicines in the treatment of diabetes mellitus.
|
208 |
23700798
|
Extracts of eleven traditional Chinese medicines (TCM) with a reputation of usefulness in treating diabetes mellitus were examined for alpha-glucosidase and alpha-amylase inhibitory activities in vitro.
|
209 |
23700798
|
To identify which constituents were responsible for the activities, thirteen triterpenoid saponins were isolated from EAT and examined for their inhibitory effects against alpha-glucosidase and alpha-amylase.
|
210 |
23700798
|
The results revealed that saponins 2, 3, 4 (IC50: 0.83 +/- 0.05 microM for BSG and IC50: 0.72 +/- 0.03 microM for SCG), 5, 6, 7, 9, 10, 11 and 12 (IC50: 1.07 +/- 0.04 micro.M for BSG and IC50: 0.93 +/- 0.05 micro.M for SCG) showed alpha-glucosidase inhibitory activities, while 2, 3, 4 (IC50: 0.93 +/- 0.04 micro.M for PPA), 5, 6, 7, 9, 10, 11 and 12 (IC50: 1.02 +/- 0.03 micro.M for PPA) possessed significant alpha-amylase inhibitory activities.
|
211 |
23700798
|
It is suggested that the glucuronic acid unit at C-3 of the aglycone is the imperative functional group of the antidiabetic activities, and two characteristic structural features are responsible for the remarkable alpha-glucosidase and alpha-amylase inhibitory activities.
|
212 |
23700798
|
alpha-Glucosidase and alpha-amylase inhibitory activities of saponins from traditional Chinese medicines in the treatment of diabetes mellitus.
|
213 |
23700798
|
Extracts of eleven traditional Chinese medicines (TCM) with a reputation of usefulness in treating diabetes mellitus were examined for alpha-glucosidase and alpha-amylase inhibitory activities in vitro.
|
214 |
23700798
|
To identify which constituents were responsible for the activities, thirteen triterpenoid saponins were isolated from EAT and examined for their inhibitory effects against alpha-glucosidase and alpha-amylase.
|
215 |
23700798
|
The results revealed that saponins 2, 3, 4 (IC50: 0.83 +/- 0.05 microM for BSG and IC50: 0.72 +/- 0.03 microM for SCG), 5, 6, 7, 9, 10, 11 and 12 (IC50: 1.07 +/- 0.04 micro.M for BSG and IC50: 0.93 +/- 0.05 micro.M for SCG) showed alpha-glucosidase inhibitory activities, while 2, 3, 4 (IC50: 0.93 +/- 0.04 micro.M for PPA), 5, 6, 7, 9, 10, 11 and 12 (IC50: 1.02 +/- 0.03 micro.M for PPA) possessed significant alpha-amylase inhibitory activities.
|
216 |
23700798
|
It is suggested that the glucuronic acid unit at C-3 of the aglycone is the imperative functional group of the antidiabetic activities, and two characteristic structural features are responsible for the remarkable alpha-glucosidase and alpha-amylase inhibitory activities.
|
217 |
23961097
|
The aim of this study was to investigate in vitro alpha-amylase enzyme inhibition by CNPG3 (2-chloro-4-nitrophenol α-d-maltotrioside) and in vivo antioxidant potential of malondialdehyde (MDA), glutathione (GSH), catalase (CAT) and total thiols (TT) in alloxan-induced diabetic rats of a methanolic extract of A. spinosus.
|