Stoĭka R S, Kusen' S I
Biokhimiia. 1979 Jul;44(7):1197-202.
The main lactate dehydrogenase (EC 1.1.1.27) isozyme from loach (Misgurnus fossilis) skeletal muscles was purified to homogeneity by polyacrylamide gel electrophoresis. The main group of lactate dehydrogenase isozymes which predominate in their activity in the unfertilized eggs of this teleost species and are stable to AgNO3 inhibition were partially purified. The effects of various concentrations of pyruvate, oxalate and urea on the activities of these purified enzyme preparations and their pH optima were studied. The antiserum for the purified lactate dehydrogenase isozyme from loach skeletal muscle was obtained. The decrease of the activity of this isozyme and that of the investigated group of isozymes from the eggs in the presence of increasing concentrations of antiserum was estimated.
通过聚丙烯酰胺凝胶电泳将泥鳅（Misgurnus fossilis）骨骼肌中的主要乳酸脱氢酶（EC 1.1.1.27）同工酶纯化至同质。对该硬骨鱼物种未受精卵中活性占主导且对硝酸银抑制稳定的主要乳酸脱氢酶同工酶组进行了部分纯化。研究了不同浓度的丙酮酸、草酸盐和尿素对这些纯化酶制剂活性及其最适pH值的影响。获得了针对泥鳅骨骼肌纯化乳酸脱氢酶同工酶的抗血清。评估了在抗血清浓度增加的情况下，该同工酶以及来自卵的被研究同工酶组活性的降低情况。
