Inhibition of horse liver alcohol dehydrogenase by methyltin compoundsстатья

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Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.

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[1] Bychkov P. V., Shekhovtsova T. N., Milaeva E. R. Inhibition of horse liver alcohol dehydrogenase by methyltin compounds // Bioinorganic Chemistry and Applications. — 2005. — Vol. 2005, no. 3-4. — P. 191–199. The study of inorganic tin (SnCl2, SnCl4) and methyltin compounds (MeSnCl3, Me2SnCI2, Me 3SnCl)effects on the enzymatic activity of alcohol dehydrogenase (ADH) in the reaction of ethanol oxidation hasbeen carried out. The experimental results of the study show that inorganic tin and methyltin substancesinduce slight inhibition of the catalytic activity of horse liver alcohol dehydrogenase (HLADH), unable to beimproved during pre-incubation with the enzyme. The conditions for carrying out the kinetic investigation ofthe mentioned phenomenon were optimized and as it turned out the mechanism of methyltin trichlorideaction, as the most effective methyltin inhibitor, is more complex than the proposed interaction of the metalatom with SH-groups of the enzyme protein. It was demonstrated that the tin compounds act in the samemanner as methylmercury compounds and might serve as oxidative agents towards the co-enzyme NADH.Kinetic data on MeSnCl3 were calculated. Data acquired on NAD-dependent ADH from horse liver and thoseregarding NAD-dependent LDH from sturgeon liver were compared. [ DOI ]

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