Lactate Dehydrogenase Isozymes: Dissociation and Recombination of Subunits
- 21 June 1963
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 140 (3573) , 1329-1330
- https://doi.org/10.1126/science.140.3573.1329
Abstract
Lactate dehydrogenase from beef tissues may be resolved electrophoretically into five isozymes each of which is a tetramer. These tetramers can be dissociated into monomers by freezing in 1M sodium chloride. On thawing, reassociation into functional tetramers occurs. On the basis of charge and amino acid composition there are two kinds of monomers. Lactate dehydrogenase-1 contains one kind of monomer and lactate dehydrogenase-5 the other kind. A mixture of equal quantities of these two isozymes, after dissociation and reassociation, leads to the production of all five isozymes in the expected proportions of 1:4:6:4:1.This publication has 11 references indexed in Scilit:
- IMMUNOCHEMICAL PROPERTIES OF LACTATE DEHYDROGENASE ISOZYMESAnnals of the New York Academy of Sciences, 1963
- Lactic Dehydrogenases: Subfractionation of IsozymesScience, 1963
- Lactate Dehydrogenases in Human TestesScience, 1963
- Isozymic patterns and properties of lactate dehydrogenase from developing tissues of the chickenJournal of Experimental Zoology, 1963
- The ontogeny of isozyme patterns of lactate dehydrogenase in the mouseDevelopmental Biology, 1962
- Physico-chemical Properties of Lactic DehydrogenaseJournal of Biological Chemistry, 1962
- Nature and Development of Lactic DehydrogenasesScience, 1962
- Dissociation of lactate dehydrogenase into subunits with guanidine hydrochlorideBiochemical and Biophysical Research Communications, 1961
- PHYSICOCHEMICAL NATURE OF ISOZYMES*Annals of the New York Academy of Sciences, 1961
- The Electrophoretically Distinct Forms of Mammalian Lactic DehydrogenasePublished by Elsevier ,1960