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dc.contributor.authorZhou, XW
dc.contributor.authorChen, Z
dc.contributor.authorChen, QX
dc.contributor.author陈清西
dc.contributor.authorYe, JL
dc.contributor.author叶剑良
dc.contributor.authorHuang, PQ
dc.contributor.authorWu, QY
dc.date.accessioned2011-10-31T10:24:40Z
dc.date.available2011-10-31T10:24:40Z
dc.date.issued2000
dc.identifier.citationSheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2000;32(2):133-138.zh_CN
dc.identifier.issn0582-9879
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/11091
dc.description.abstractIn order to study the structure-activity relationship and molecular mechanism of insulin-mimetic peroxovanadium complexes, the low-molecular-weight BHPTPase from bovine heart has been purified mainly by chromatography of DEAE-cellulose and Sephadex G-75, which was showed homogenicity on SDS-PAGE. Four bioactive peroxovanadium(pV) complexes bpV(ox), bpV(bipy), bpV(phen) and bpV(pic), [VO(O-2)(2)L](n-), where L = oxalic acid dianion(ox), bipyridine(bipy), 1, 10-phenanthroline(phen), pyridine-2-carboxylic acid (pic) have been synthesized; the bonding properties of center metal and its ligand were characterized by V-51 NMR, C-13 NMR, IR and elemental analysis. The complexes displayed remarkable inhibitory effects on the bovine heart tyrosine phosphatase. Their IC50 were 0.22, 0.36, 0.90 and 0.28 mu mol/L, respectively. The structure-activity relationship of the complexes were discussed by their oxidizing ability and through the steric space hindrance of the organic ligands.zh_CN
dc.language.isoenzh_CN
dc.publisherSHANGHAI INST BIOCHEMISTRY, ACADEMIA SINICAzh_CN
dc.subjectperoxovanadium complexeszh_CN
dc.subjecttyrosine phosphatasezh_CN
dc.subjectinhibitionzh_CN
dc.subjectstructure-activity relationshipzh_CN
dc.titleInhibition effects of some bioactive peroxovanadium complexes on the tyrosine phosphatasezh_CN
dc.typeArticlezh_CN


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