ABSTRACT The primary and tertiary structure of vertebrate LDH-A (muscle), LDH-B (heart) and LDH-C (testis) are compared, and the amino acid sequence differences among three types of isozymes are related to their unique enzymatic properties. The sequence changes of human LDH-A and LDH-B mutant proteins are specifically correlated to their enzymatic activities. Functions of LDH as structural protein of lens and single-stranded DNA-binding proteins are discussed. Molecular evolution of vertebrate LDH-A, LDH-B and LDH-C isozymes are briefly reviewed.
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