Vanchugova L V, Valueva T A, Romashkin V I, Rozenfel'd M A, Valuev L I
Biokhimiia. 1988 Sep;53(9):1455-61.
The interaction of highly purified duck egg white ovomucoid with trypsin and chymotrypsin was studied. It was found that the ovomucoid molecule contains two equally effective trypsin-binding sites which, in their turn, comprise lysine residues and one independent chymotrypsin-binding site. The values of inhibition constants were determined and the changes in free energy, enthalpy and entropy during the ovomucoid interaction with trypsin and chymotrypsin were established. It was shown that the inhibitor affinity for the enzymes does not change at low degrees of free amino groups modification.
研究了高纯度鸭蛋清卵类粘蛋白与胰蛋白酶和糜蛋白酶的相互作用。发现卵类粘蛋白分子含有两个同等有效的胰蛋白酶结合位点，这些位点依次包含赖氨酸残基和一个独立的糜蛋白酶结合位点。测定了抑制常数的值，并确定了卵类粘蛋白与胰蛋白酶和糜蛋白酶相互作用过程中的自由能、焓和熵的变化。结果表明，在游离氨基修饰程度较低时，抑制剂对酶的亲和力不变。
