乳酸脱氢酶同功酶的精子细胞和测试。
文章的细节
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引用
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克劳森J
乳酸脱氢酶同功酶的精子细胞和测试。
j . 1969年1月,111 (2):207 - 18。
- PubMed ID
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4303363 (在PubMed]
- 文摘
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1。乳酸脱氢酶同工酶LDH的动力学和代谢特性(x)从人类精子细胞和大鼠睾丸进行了研究。2。LDH (x)显示了一个由stilboestrol敏感抑制二磷酸,尿素和氯化胍盐不同的LDH-H(4)和LDH-M(4)同功酶。3所示。大约10和总数的20%乳酸脱氢酶活性分别为睾丸和精子细胞与颗粒分数有关。在精子细胞11%本地化的中段和18.8%的分数。LDH (x)被发现在所有颗粒分数的精子细胞。中间一块包含LDH总额的41.0% (x)活动和显示高琥珀酸脱氢酶活性。5。 The pH-dependence of lactate/pyruvate and NAD(+)/NADH concentration ratios were estimated. Lactate dehydrogenase in sperm cells has maximal activity with NADH as coenzyme at pH7.5 and with NADPH as coenzyme at pH6.0. At pH6.0 a 10% greater oxidation of NADPH than of NADH was found. At acid pH lactate hydrogenase may function as an enzyme bringing about transhydrogenation from NADPH to NAD(+). 6. In agreement with the stoicheiometry of the lactate de- hydrogenase reaction, the lactate/pyruvate concentration ratio decreased with increasing pH. 7. The lactate/pyruvate and NAD(+)/NADH concentration ratios were estimated with glucose, fructose and sorbitol as substrates and as a function of time after addition of these substrates. During a 20min. period after the addition of the substrates, changes in lactate/pyruvate and NAD(+)/NADH concentration ratios were noticed. Increasing concentration of the substrates mentioned gave rise to asymptotic increases in lactate and pyruvate. 8. Sorbitol did not act as a substrate for LDH(x). 9. The findings described are consistent with the idea that LDH(x) is different from other known lactate dehydrogenase isoenzymes, but that it has a metabolic function similar to that of the isoenzymes of other tissues.
DrugBank数据引用了这篇文章
- 药物靶点
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药物 目标 类 生物 药理作用 行动 NADH L-lactate脱氢酶B链 蛋白质 人类 未知的不可用 细节