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pubmed-article:15143515pubmed:issue6lld:pubmed
pubmed-article:15143515pubmed:dateCreated2004-5-17lld:pubmed
pubmed-article:15143515pubmed:abstractTextThe effect of L-cysteine on activity of hydrophobic forms of calf intestine alkaline phosphatase was investigated. Apparent inhibition constants for mixed type inhibition have been determined. The kinetic results allow supposing that the mechanism of equilibrium establishment between the inhibitor and enzyme involves the initial rapid formation of intermediate complex and a subsequent slower step leading to its stabilization in the substrate binding site. The microscopic rate constants for slow step of interaction of L-cysteine with alkaline phosphatase have been calculated. Effect of pH on apparent inhibition constants and kinetic parameters for enzymatic reaction in the presence of L-cysteine was analysed.lld:pubmed
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pubmed-article:15143515pubmed:issn0201-8470lld:pubmed
pubmed-article:15143515pubmed:authorpubmed-author:VovkA IAIlld:pubmed
pubmed-article:15143515pubmed:authorpubmed-author:KharchenkoO...lld:pubmed
pubmed-article:15143515pubmed:authorpubmed-author:MuzychkaO VOVlld:pubmed
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pubmed-article:15143515pubmed:volume75lld:pubmed
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pubmed-article:15143515pubmed:pagination35-9lld:pubmed
pubmed-article:15143515pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15143515pubmed:articleTitle[Kinetic and mechanism of interaction of L-cysteine with alkaline phosphatase from calf intestines].lld:pubmed
pubmed-article:15143515pubmed:affiliationInstitute of Bioorganic Chemistry and Petrochemistry, National Academy of Sciences of Ukraine, Kyiv. vovk@bpci.kiev.ualld:pubmed
pubmed-article:15143515pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15143515pubmed:publicationTypeEnglish Abstractlld:pubmed