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Synergetic inhibition of metal ions and genistein on α‐glucosidase
Author(s) -
Wang Yufang,
Ma Lin,
Li Zhong,
Du Zhiyun,
Liu Zhong,
Qin Jiangke,
Wang Xiaodong,
Huang Zhishu,
Gu Lianquan,
Chen Albert S.C.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.08.059
Subject(s) - genistein , chemistry , metal ions in aqueous solution , metal , kinetics , ion , nuclear chemistry , non competitive inhibition , inhibitory postsynaptic potential , inorganic chemistry , enzyme , biochemistry , organic chemistry , biology , physics , quantum mechanics , neuroscience , endocrinology
Inhibition of metal ions and synergetic inhibition of metal ions/genistein on α‐glucosidase activity has been investigated. We have examined the inhibitory effect of Cu 2+ , Ni 2+ , Mg 2+ , Fe 2+ , Hg 2+ , Zn 2+ , Ca 2+ , Pb 2+ , Ag + , V 5+ , V 4+ and Mn 2+ ions. The results show that the nature of the inhibition was reversible, slow‐binding, non‐competitive, and the K i values of some ions such as Cu 2+ , Ni 2+ and Zn 2+ range from 10 −5 to 10 −6 M. Moreover, synergetic inhibitory effect of metal ions and genistein on α‐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 α‐glucosidase at the same time. Furthermore, the mechanism of the synergetic inhibition was examined by spectrophotometry.