Calorimetric study of inhibition of urease by 2-mercaptoethanol - Procedures based upon integrated rate equations

被引：5

作者：

Juszkiewicz, A ^{[1
]}

Kot, M ^{[1
]}

Zaborska, W ^{[1
]}

机构：

[1] Jagiellonian Univ, Fac Chem, PL-30060 Krakow, Poland

来源：

THERMOCHIMICA ACTA | 1998年 / 320卷 / 1-2期

关键词：

enzymatic calorimetry; 2-mercaptoethanol; urease; urease inhibition;

D O I：

10.1016/S0040-6031(98)00397-9

中图分类号：

O414.1 [热力学];

学科分类号：

摘要：

Urease-catalyzed hydrolysis of urea was studied in the absence, and presence, of 0.3 and 0.8 mmol dm(-3) 2-mercaptoethanol in phosphate buffer at pH 7.0 at 25 degrees C with the use of an isoperibol calorimeter. The extent of reaction with time, Delta T vs. t, was interpreted with the help of the integrated Michaelis-Menten equation, and the inhibition constant K-i was obtained from linear transformations of the equation (Jennings-Niemann, Yun-Suelter and Booman-Niemann). The obtained value of K-i was equal to 0.87+/-0.10 mmol dm(-3). (C) 1998 Elsevier Science B.V.

引用

页码：45 / 52

页数：8

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