Lindenbaum G M, Bogacheva T I, Mirgorodskaia O A, Moskvichev B V, Tereshin I M
Prikl Biokhim Mikrobiol. 1977 Sep-Oct;13(5):685-91.
The molecular weight distribution, thermal stability during autolysis, resistance to human serum inhibitors as well as temperature optimum of native and dextran-modified trypsin were investigated. The seeming constants of autolytic inactivation and inhibition of native and modified trypsin were calculated. Trypsin polymer derivatives had higher molecular weight than the native enzyme. They also showed higher resistance to autolysis and serum inhibitors. Possible causes of the above effects are discussed.
研究了天然胰蛋白酶和葡聚糖修饰胰蛋白酶的分子量分布、自溶过程中的热稳定性、对人血清抑制剂的抗性以及最适温度。计算了天然和修饰胰蛋白酶自溶失活和抑制的表观常数。胰蛋白酶聚合物衍生物的分子量高于天然酶。它们对自溶和血清抑制剂也表现出更高的抗性。讨论了上述效应的可能原因。
