Abstract
ELECTROPHORESIS usually reveals five lactic dehydrogenase (LDH) isoenzymes in vertebrate tissues. Each isoenzyme is considered to be a tetramer, usually composed of two sub-units, polypeptide monomers A (LDH5) and B (LDH1). Genetic evidence1–3 indicates that synthesis of the polypeptides is controlled by two loci, A and B. In testis and spermatozoa from different animals, with the exception of pigs4,5, six to eight fractions were discovered. The extra bands were named x-bands. Zinkham and Blanco6 found that the LDHx-band in pigeon testis is polymorphic, and concluded that this is controlled by a third locus C. Ressler et al.7 suggested that LDHx-band in human spermatozoa is formed from A and B sub-units and some other compound. Zinkham et al.4 and Goldberg5 found that in vitro sub-units of LDHX can produce mixed forms with sub-units A and B.
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VALENTA, M., HYLDGAAKD-JENSEN, J. & MOUSTGAARD, J. Three Lactic Dehydrogenase Isoenzyme Systems in Pig Spermatozoa and the Polymorphism of Sub-units controlled by a Third Locus C. Nature 216, 506–507 (1967). https://doi.org/10.1038/216506a0
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DOI: https://doi.org/10.1038/216506a0
