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一种用于检测C1酯酶抑制剂的动力学试验。

A kinetic test for the assay of the C1 esterase-inhibitor.

作者信息

Schena F P, Manno C, D'Agostino R, Bruno G, Cramarossa F, Bonomo L

出版信息

J Clin Chem Clin Biochem. 1980 Jan;18(1):17-21. doi: 10.1515/cclm.1980.18.1.17.

Abstract

The most satisfactory diagnostic procedure for hereditary angioneurotic oedema is the demonstration of low serum levels of C1 esterase-inhibitor. A modified method for the assay of this protein is described. It is based on the kinetic measurement of the C1 esterase-inhibitor when it inhibits the hydrolysis of N-acetyl-L-tyrosine-ethyl ester by C1 esterase. The relative C1 esterase-inhibitor concentration is based on the initial hydrolytic velocity, which can be evaluated from the pH change in a short time and within a small range. High reproducibility, cheap instrumentation and short time of analysis are some of the favorable aspects of this method in comparison with the 'end point titrimetric' method. Furthermore, this paper describes the mechanism of inhibition of C1 esterase by C1 esterase-inhibitor. The results are indicative of a non-competitive mechanism. The value of the Michaelis-Menten constant, Km, is 0.017 +/- 0.001 mol/l at 37 degrees C, in the optimum pH range 7.2-7.4. An estimate of KI in arbitrary units is also given.

摘要

对于遗传性血管性水肿,最令人满意的诊断方法是证明血清中C1酯酶抑制剂水平较低。本文描述了一种用于检测该蛋白的改良方法。它基于在C1酯酶抑制剂抑制C1酯酶水解N-乙酰-L-酪氨酸乙酯时对C1酯酶抑制剂的动力学测量。相对C1酯酶抑制剂浓度基于初始水解速度,该速度可在短时间内和小范围内通过pH变化进行评估。与“终点滴定法”相比,该方法具有重现性高、仪器成本低和分析时间短等优点。此外,本文还描述了C1酯酶抑制剂对C1酯酶的抑制机制。结果表明这是一种非竞争性机制。在37℃、最佳pH范围7.2 - 7.4时,米氏常数Km的值为0.017±0.001 mol/l。文中还给出了任意单位下KI的估计值。

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A kinetic test for the assay of the C1 esterase-inhibitor.一种用于检测C1酯酶抑制剂的动力学试验。
J Clin Chem Clin Biochem. 1980 Jan;18(1):17-21. doi: 10.1515/cclm.1980.18.1.17.

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