1979
DOI: 10.1530/jrf.0.0550101
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Substrate specificity of the lactate dehydrogenase isoenzyme C4 from human spermatozoa and a possible selective assay

Abstract: The activity of lactate dehydrogenase (EC 1.1.1.27) in normal human sperm lysates and in human heart and liver homogenates was determined by using a variety of 2-oxoacids as substrates. Sperm preparations were active with pyruvate, 2-oxobutanoate, 2-oxopentanoate and 2-oxohexanoate, while heart and liver extracts utilized only pyruvate and 2-oxobutanoate. Selective staining after gel electrophoresis indicated that the fraction corresponding to lactate dehydrogenase C4, the sperm-specific isoenzyme, was respons… Show more

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Cited by 24 publications
(15 citation statements)
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“…7,8,10,21 All LDH isozymes catalyse the reaction from pyruvate to lactate and from lactate to pyruvate. However, the LDH-C4 shows activity towards α-keto and α-hydroxy acid, of longer carbon chain than those of pyruvate and lactate (Figure 1).…”
Section: Discussionmentioning
confidence: 99%
“…7,8,10,21 All LDH isozymes catalyse the reaction from pyruvate to lactate and from lactate to pyruvate. However, the LDH-C4 shows activity towards α-keto and α-hydroxy acid, of longer carbon chain than those of pyruvate and lactate (Figure 1).…”
Section: Discussionmentioning
confidence: 99%
“…Therefore, the determination of LDH-X in the semen can represent a reliable index of sperm quality [2, 41. The assay of total LDH activity does not give a direct estimate of LDH-X values; an electrophoretic enzymogram is necessary to measure, by densitometry , the relative proportions of each isoenzyme. Some investigators [2] have viewed this procedure as unduly complex, and requiring excessive time for routine clinical usage. Furthermore, many clinical laboratories do not have easy access to the technology necessary for this assay.…”
Section: Discussionmentioning
confidence: 99%
“…Furthermore, many clinical laboratories do not have easy access to the technology necessary for this assay. The solution to this problem has been a selective assay for LDH-X using substrates for which it has higher affinity than the rest of LDH isoenzymes [2,8,9]. Within this concept, the strong affinity shown by LDH-X for a-ketobutyrate has allowed us to measure the levels of HBDH and establish the ratio HBDHILDH, whose estimation is simple, rapid, sensitive, available to any laboratory, and appears to be a more accessible technique for looking at LDH-X activity.…”
Section: Discussionmentioning
confidence: 99%
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