Synergetic inhibition of metal ions and genistein on alpha-glucosidase.
Inhibition of metal ions and synergetic inhibition of metal ions/genistein on alpha-glucosidase activity has been investigated. We have examined the inhibitory effect of Cu2+, Ni2+, Mg2+, Fe2+, Hg2+, Zn2+, Ca2+, Pb2+, Ag+, V5+, V4+ and Mn2+ ions. The results show that the nature of the inhibition was reversible, slow-binding, non-competitive, and the Ki values of some ions such as Cu2+, Ni2+ and Zn2+ range from 10(-5) to 10(-6) M. Moreover, synergetic inhibitory effect of metal ions and genistein on alpha-glucosidase were studied with kinetics method. It is concluded that the inhibitory effect was much greater when both of them were added to the reactant solution simultaneously than that they were added, respectively, which suggests that the inhibitors seem to bind to the different sites of alpha-glucosidase at the same time. Furthermore, the mechanism of the synergetic inhibition was examined by spectrophotometry.
Wang
Yufang
Y
School of Chemistry and Chemical Engineering, SUN Yat-sen (Zhongshan) University, 510275 Guangzhou, China.
Ma
Lin
L
Li
Zhong
Z
Du
Zhiyun
Z
Liu
Zhong
Z
Qin
Jiangke
J
Wang
Xiaodong
X
Huang
Zhishu
Z
Gu
Lianquan
L
Chen
Albert S C
AS
D002118:Calcium / Q000494:pharmacology*; D002412:Cations / Q000737:chemistry; D002942:Circular Dichroism; D004305:Dose-Response Relationship, Drug; D004357:Drug Synergism; D019833:Genistein / Q000494:pharmacology*; D065089:Glycoside Hydrolase Inhibitors; D007700:Kinetics; D019216:Metals, Heavy / Q000494:pharmacology*; D017433:Protein Structure, Secondary; D000520:alpha-Glucosidases / Q000737:chemistry
D002412:Cations; D065089:Glycoside Hydrolase Inhibitors; D019216:Metals, Heavy; D019833:Genistein; D000520:alpha-Glucosidases; D002118:Calcium