Inhibitory Mechanism of Apigenin on α-Glucosidase and Synergy Analysis of Flavonoids
Author:
Affiliation:
1. State Key Laboratory of Food Science, Technology, Nanchang University, Nanchang 330047, China
2. School of Biological Sciences, The University of Auckland, Auckland 1142, New Zealand
Funder
National Natural Science Foundation of China
Natural Science Foundation of Jiangxi Province
Department of Education of Jiangxi Province
State Key Laboratory of Food Science and Technology, Nanchang University
Publisher
American Chemical Society (ACS)
Subject
General Agricultural and Biological Sciences,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jafc.6b02314
Reference52 articles.
1. Biochemical properties and substrate recognition mechanism of GH31 α-glucosidase from Bacillus sp. AHU 2001 with broad substrate specificity
2. Structural Basis for Substrate Selectivity in Human Maltase-Glucoamylase and Sucrase-Isomaltase N-terminal Domains
3. Pu-erh tea polysaccharides decrease blood sugar by inhibition of α-glucosidase activity in vitro and in mice
4. Bean cultivars (Phaseolus vulgaris L.) have similar high antioxidant capacity, in vitro inhibition of α-amylase and α-glucosidase while diverse phenolic composition and concentration
5. α-Glucosidase and tyrosinase inhibitory effects of an abietane type diterpenoid taxoquinone from Metasequoia glyptostroboides
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