器官特异性与乳酸脱氢酶活性。人类精子乳酸脱氢酶的一些特性。
Organ specificity and lactate-dehydrogenase activity. Some properties of human spermatozoal lactate dehydrogenase.
作者信息
Wilkinson J H, Withycombe W A
出版信息
Biochem J. 1965 Dec;97(3):663-8. doi: 10.1042/bj0970663.
Abstract
- 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.
摘要
- 通过在醋酸纤维素和聚丙烯酰胺凝胶上进行电泳，已证实人、小鼠和犬的睾丸以及人类精子中存在一种特征性乳酸脱氢酶同工酶（LD(x)）。2. 人类精子同工酶对2-氧代丁酸的亲和力比在其他组织中发现的五种同工酶中的任何一种都高得多。丙酮酸的K(m)值为0.05mmol/L，2-氧代丁酸的K(m)值为0.18mmol/L。3. LD(x)与其他乳酸脱氢酶同工酶不同，其性质与其电泳迁移率无关。它与LD(1)相似，受到0.2mmol/L草酸盐的强烈抑制，对2mol/L尿素相对抗性，并且对热相对稳定。4. LD(x)对2-氧代丁酸具有惊人的高活性，这表明该物质或2-羟基丁酸可能在精子代谢中起作用。
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