Burgos C, Gerez de Burgos N M, Coronel C E, Blanco A
J Reprod Fertil. 1979 Jan;55(1):101-6. doi: 10.1530/jrf.0.0550101.
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 responsible for the utilization of substrates with a linear chain of 3 to 6 carbon atoms. The use of 5 mM 2-oxohexanoate allowed the selective determination of isoenzyme C4 in preparations containing different lactate dehydrogenase molecular forms.
通过使用多种2-氧代酸作为底物，测定了正常人精子裂解物以及人心脏和肝脏匀浆中乳酸脱氢酶（EC 1.1.1.27）的活性。精子制剂对丙酮酸、2-氧代丁酸、2-氧代戊酸和2-氧代己酸有活性，而心脏和肝脏提取物仅利用丙酮酸和2-氧代丁酸。凝胶电泳后的选择性染色表明，与精子特异性同工酶乳酸脱氢酶C4相对应的组分负责利用具有3至6个碳原子直链的底物。使用5 mM 2-氧代己酸可在含有不同乳酸脱氢酶分子形式的制剂中选择性测定同工酶C4。
