PMID: 5894044Dec 1, 1965

Organ specificity and lactate-dehydrogenase activity. Some properties of human spermatozoal lactate dehydrogenase

The Biochemical Journal
J H WILKINSON, W A WITHYCOMBE

Abstract

1. The presence of a characteristic lactate-dehydrogenase isoenzyme (LD(x)) in human, mouse and dog testis and in human spermatozoa has been confirmed by electrophoresis on cellulose acetate and on polyacrylamide gel. 2. The human spermatozoal isoenzyme exhibits a much higher affinity for 2-oxobutyrate than any of the five isoenzymes found in other tissues. K(m) values of 0.05mm for pyruvate and 0.18mm for 2-oxobutyrate were obtained. 3. LD(x) differs from other lactate-dehydrogenase isoenzymes in that its properties cannot be correlated with its electrophoretic mobility. It resembles LD(1) in being strongly inhibited by 0.2mm-oxalate and relatively resistant to 2m-urea, and in being relatively stable to heat. 4. The surprisingly high activity of LD(x) with 2-oxobutyrate suggests that this substance or 2-hydroxybutyrate may play a part in spermatozoal metabolism.

Citations

Jun 1, 1970·The Journal of Experimental Zoology·L J Battellino, A Blanco
Aug 1, 1970·The Journal of Experimental Zoology·C Hawtrey, E Goldberg
Aug 12, 2015·International Journal of Environmental Research and Public Health·Yang WangLinna Wei
Jan 12, 2016·International Journal of Molecular Sciences·Yang WangLinna Wei
Feb 18, 1967·Nature·M R Banner, S B Rosalki
Apr 1, 1967·The Journal of Experimental Zoology·E Goldberg, C Hawtrey
Jul 1, 1969·Zeitschrift für Ernährungswissenschaft·J Clausen
Dec 31, 2019·Endocrine, Metabolic & Immune Disorders Drug Targets·Amjad Ali KhanArshad Husain Rahmani
May 1, 1974·Annals of Clinical Biochemistry·M J McQueen

Related Concepts

butyrate
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Electrophoresis
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Lactate Dehydrogenase
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Tissue Specificity

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