人血浆中α-抑制因子对人及牛胰蛋白酶和胰凝乳蛋白酶抑制作用的动力学研究。
A kinetic study of the inhibition of human and bovine trypsins and chymotrypsins by the inter-alpha-inhibitor from human plasma.
作者信息
Aubry M, Bieth J
出版信息
Biochim Biophys Acta. 1976 Jun 7;438(1):221-30. doi: 10.1016/0005-2744(76)90238-2.
Human plasma inter-alpha-inhibitor forms 1:1 inactive complexes with human and bovine trypsins (EC 3.4.21.4) and chymotrypsins (EC 3.4.21.1). The association and dissociation rate constants as well as the equilibrium dissociation constants (Ki) of the complexes formed of inter-alpha-inhibitor and the four proteases have been measured. The most stable complexes are those formed with the bovine enzymes. For instance, Ki = 2.1-10-11 M for bovine trypsin whereas Ki = 1.2 - 10-8 M for human trypsin. Whatever the species, the complexes formed with the chymotrypsins are less stable than those formed with the trypsins.
人血浆α-抑制因子间体与人和牛的胰蛋白酶（EC 3.4.21.4）及胰凝乳蛋白酶（EC 3.4.21.1）形成1:1的无活性复合物。已测定了α-抑制因子间体与这四种蛋白酶形成的复合物的缔合和解离速率常数以及平衡解离常数（Ki）。最稳定的复合物是与牛酶形成的复合物。例如，牛胰蛋白酶的Ki = 2.1×10⁻¹¹ M，而人胰蛋白酶的Ki = 1.2×10⁻⁸ M。无论何种物种，与胰凝乳蛋白酶形成的复合物都不如与胰蛋白酶形成的复合物稳定。
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