Abstract
RECOGNITION of the molecular heterogeneity of enzymes in single organisms has offered a new dimension for studying the genetic control of enzyme synthesis. In the case of lactate dehydrogenase (LDH) five distinct types (isozymes) can be identified in most mammalian and avian tissues by the method of starch-gel electrophoresis1–3. Each isozyme is a tetramer formed by the association of two monomers, A and B (ref. 4), so that the polypeptide composition of LDH–1 through LDH–5 respectively may be written as follows: A0B4, A1B3, A2B2, A3B1 and A4B0. Genetic investigations5–7 have shown that the synthesis of the A and B sub-units is under the control of two different structural genes, a and b. Hence the isozyme composition of each tissue depends on the relative activity of the genes at these loci.
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ZINKHAM, W., KUPCHYK, L., BLANCO, A. et al. Polymorphism of Lactate Dehydrogenase Isozymes in Pigeons. Nature 208, 284–286 (1965). https://doi.org/10.1038/208284a0
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DOI: https://doi.org/10.1038/208284a0
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