Akihama S, Matsuda Y, Fukase T, Yamanaka A, Okude M
Department of Biochemistry, Meiji College of Pharmacy, Tokyo, Japan.
Yakugaku Zasshi. 1995 Jul;115(7):537-42. doi: 10.1248/yakushi1947.115.7_537.
In order to estimate the effects of sialic acid residues in fibrinogen on the fibrinogen-fibrin conversion by bovine thrombin the Michaelis constant (Km) and maximum velocity (Vmax) were determined. The Km value obtained by the use of intact-fibrinogen was smaller than that of asialo-fibrinogen. This fact suggests that the sialic acid residues affected the formation of the enzyme-substrate complex. It was also found that in comparison with the asialo-fibrinogen, the intact-fibrinogen was significantly influenced in the gel formation time by the ionic strength in the reaction solution.
为了评估纤维蛋白原中唾液酸残基对牛凝血酶介导的纤维蛋白原 - 纤维蛋白转化的影响，测定了米氏常数（Km）和最大反应速度（Vmax）。使用完整纤维蛋白原获得的Km值小于去唾液酸纤维蛋白原的Km值。这一事实表明，唾液酸残基影响了酶 - 底物复合物的形成。还发现，与去唾液酸纤维蛋白原相比，完整纤维蛋白原在反应溶液中的离子强度对凝胶形成时间有显著影响。
