Busquets M, Cortés A, Bozal J
Int J Biochem. 1985;17(7):825-9. doi: 10.1016/0020-711x(85)90271-x.
A method for the purification of chicken liver soluble aspartate aminotransferase, lactate dehydrogenase free, is proposed. The preparation, which contained a mixture of the five molecular forms of the enzyme, showed a 120-fold increase in specific activity, with respect to the initial homogenates. Differences in Km(2-oxoglutarate) and saturating concentrations among solutions of purified enzyme and soluble fraction were due to the 2-oxoglutarate reductase activity of lactate dehydrogenase.
提出了一种纯化鸡肝可溶性天冬氨酸转氨酶(不含乳酸脱氢酶)的方法。该制剂含有该酶五种分子形式的混合物,其比活性相对于初始匀浆提高了120倍。纯化酶溶液和可溶级分之间在Km(2-氧代戊二酸)和饱和浓度方面的差异是由于乳酸脱氢酶的2-氧代戊二酸还原酶活性所致。