Bogacheva T I, Mirgorodskaia O A, Moskvichev B V
Biokhimiia. 1977 Apr;42(4):609-15.
Physico-chemical properties of trypsin covalently bound with human serum albumin by glutaric aldehyde have been studied. The modification of the enzyme practically caused no changes in the pH optimum of trypsin. The inhibition of modified trypsin by inhibitors from soy beans and human blood serum has been also studied. The apparent inhibition constants have been calculated. The modification has been shown to result in a deceleration of autolytic degradation. The autolysis rate constants have been calculated at 50 degrees C.
对通过戊二醛与人血清白蛋白共价结合的胰蛋白酶的物理化学性质进行了研究。酶的修饰实际上未引起胰蛋白酶最适pH值的变化。还研究了来自大豆和人血清的抑制剂对修饰胰蛋白酶的抑制作用。计算了表观抑制常数。已表明修饰导致自溶降解减速。在50℃下计算了自溶速率常数。
