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Maleimideinactivation of lactate dehydrogenase isozymes

descriptionPublicationkeyboard_double_arrow_right Article 01 May 1974 English Publisher:Elsevier BVJournal:Biochimica et Biophysica Acta (BBA) - Enzymology, volume 350, pages 135-140 (issn: 0005-2744,

Authors: Sharon V. Vercellotti; Tom L. Fisher; Bruce M. Anderson;

doi: 10.1016/0005-2744(74)90211-3

pmid: 4366385

Maleimideinactivation of lactate dehydrogenase isozymes

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Abstract

Abstract The homologous beef lactate dehydrogenase (EC 1.1.1.27) isozymes H 4 and M 4 were observed to be effectively inactivated by a homologous series of N- alkylmaleimides . With each isozyme, the second-order rate constants of inactivation increased with increasing chain length of the alkyl group of the maleimide derivative. The rate of inactivation of lactate dehydrogenase (H 4 ) by N- heptylmaleimide was decreased in the presence of NADH while no protective effect by NADH was noted in the inactivation of lactate dehydrogenase (M 4 ) by this maleimide. Adenosine, AMP, ADP and adenosine diphosphoribose were shown to be coenzyme-competitive inhibitors of both lactate dehydrogenase (H 4 ) and lactate dehydrogenase (M 4 ). Binding patterns of these compounds were very similar with the two isozymes studied.

Related Organizations

Virginia Tech
United States

Keywords

Adenosine, Binding Sites, Time Factors, L-Lactate Dehydrogenase, Nucleoside Diphosphate Sugars, Myocardium, Ribose, NAD, Binding, Competitive, Adenosine Monophosphate, Adenosine Diphosphate, Isoenzymes, Maleimides, Kinetics, Structure-Activity Relationship, Oxidation-Reduction, Protein Binding

1 Research products, page 1 of 1

Inactivation of chicken liver d-3-phosphoglycerate dehydrogenase by N-alkylmaleimides
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