Valueva T A, Kladnitskaya G V, Mosolov V V
A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
Immunopharmacology. 1996 May;32(1-3):108-10. doi: 10.1016/0162-3109(95)00066-6.
A serine proteinase inhibitor (ovomucoid) has been isolated from duck egg white. The duck ovomucoid effectively inhibited HLE, PPE, chymotrypsin, and HCG in a 1:1 molar ratio, and trypsin in a 1:2 molar ratio. Inhibition of human plasmin and porcine pancreatic kallikrein was not observed. The ovomucoid shows equilibrium dissociation constants of 0.002; 2.4; 2.2; 6.1; and 18.0 nM for HLE, PPE, chymotrypsin, trypsin, and HCG, respectively. The molecule of inhibitor can simultaneously bind two trypsin molecules and one molecule of elastase (or chymotrypsin).
已从鸭蛋清中分离出一种丝氨酸蛋白酶抑制剂（卵类粘蛋白）。鸭卵类粘蛋白能以1:1的摩尔比有效抑制人白细胞弹性蛋白酶（HLE）、猪胰弹性蛋白酶（PPE）、胰凝乳蛋白酶和人绒毛膜促性腺激素（HCG），并以1:2的摩尔比抑制胰蛋白酶。未观察到对人纤溶酶和猪胰激肽释放酶的抑制作用。卵类粘蛋白对HLE、PPE、胰凝乳蛋白酶、胰蛋白酶和HCG的平衡解离常数分别为0.002、2.4、2.2、6.1和18.0 nM。该抑制剂分子可同时结合两个胰蛋白酶分子和一个弹性蛋白酶（或胰凝乳蛋白酶）分子。
