Formation of human lactate dehydrogenase isozyme patterns in vitro.

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Abstract
Human LDH [lactate dehydrogenase] isozyme patterns have been formed in vitro by mixing different proportions of LDH 1 and LDH 5 in high salt concentration and freezing the mixtures for 4 hr. according to the method described Markert. Neither presence of several common intracellular metabolites, substrates, and coenzymes nor dilution of mixtures containing LDH 1 and LDH 5 in fixed proportions significantly altered the isozyme patterns obtained on recombination. Several polyhydroxy compounds prevented recombination on freezing, but failed to protect LDH activity at 25[degree]C from inhibition by 4 [image] urea. These results suggest that random recombination of subunits may be a principal mechanism for isozyme production in vivo. Alternative mechanisms controlling formation of isozyme patterns in vivo are discussed.