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.