Leĭbman D Ia, Nesterov V P
Biokhimiia. 1979 May;44(5):822-31.
The purified preparations of glyceraldehyde-3-phosphate dehydrogenase isolated from frog and pike skeletal muscles were found homogenous under polyacrylamide gel electrophoresis. Their amino acid composition is similar to that of glyceraldehyde-3-phosphate dehydrogenase from other animal species. The interaction kinetics for frog and pike glyceraldehyde-3-phosphate dehydrogenase SH-groups with 5,5'-dithio-bis-(2-nitrobenzoate) (DTNB) were studied. A negative correlation between the thermal stability of the enzyme preparations from pig, pike, lamprey and frog muscles and the reactivity of their SH-groups with respect to DTNB was observed. NAD at saturating concentrations was found to protect the enzyme from lower vertebrates muscles against thermal inactivation in a lesser degree than does the pig muscle enzyme. The weaker protective effect of NAD was observed for lamprey and frog enzyme preparations, which are characterized by a low SH-group reaction ability. Frog and pike apoenzymes are considerably more resistant to trypsin proteolysis than the pig apoenzyme.
从青蛙和狗鱼骨骼肌中分离得到的甘油醛-3-磷酸脱氢酶纯化制剂在聚丙烯酰胺凝胶电泳下呈现均一性。它们的氨基酸组成与其他动物物种的甘油醛-3-磷酸脱氢酶相似。研究了青蛙和狗鱼甘油醛-3-磷酸脱氢酶的巯基与5,5'-二硫代双-(2-硝基苯甲酸)(DTNB)的相互作用动力学。观察到猪、狗鱼、七鳃鳗和青蛙肌肉中酶制剂的热稳定性与其巯基对DTNB的反应活性之间呈负相关。发现饱和浓度的NAD对低等脊椎动物肌肉中的酶的热失活保护作用比猪肌肉酶的保护作用小。对于七鳃鳗和青蛙酶制剂，观察到NAD的保护作用较弱，其特点是巯基反应能力较低。青蛙和狗鱼的脱辅酶比猪脱辅酶对胰蛋白酶水解的抵抗力强得多。
