从胃黏膜中纯化得到的钾刺激型ATP酶的动力学特性

Kinetic properties of potassium stimulated ATPase purified from gastric mucosa.

作者信息

Tükel S, Isbir T

机构信息

University of Cukurova, Medical Faculty, Department of Biochemistry, Balcali, Adana, Turkey.

出版信息

Z Naturforsch C J Biosci. 1988 Jul-Aug;43(7-8):609-12.

PMID:2851894

Abstract

In this study, partially purified K+-H+ ATPase from frog gastric mucosa were obtained by using differential and density gradient centrifugation. Optimum activity of K+-H+ ATPase (Vmax), Michealis-Menten constant (Km) and Hill coefficient (h) were found as 83.3 mumol Pi.mg prot-1.h-1, 95.2 microM and 0.91, respectively. Enzyme preparations were more stable in glycerol solutions stored at -40 degrees C. Minimum activity lost was determined for samples stored in 40% (v/v) glycerol solution at -40 degrees C for two months.

摘要

在本研究中，通过差速离心和密度梯度离心从青蛙胃黏膜中获得了部分纯化的钾氢ATP酶。发现钾氢ATP酶的最佳活性（Vmax）、米氏常数（Km）和希尔系数（h）分别为83.3微摩尔无机磷·毫克蛋白⁻¹·小时⁻¹、95.2微摩尔和0.91。酶制剂在-40℃储存的甘油溶液中更稳定。对于在-40℃的40%（v/v）甘油溶液中储存两个月的样品，测定其活性损失最小。