人谷氨酸脱氢酶（GDH）的纯化及GDH与兔抗人GDH抗体相互作用的吸附伏安法研究

Purification of human glutamate dehydrogenase (GDH) and an adsorptive voltammetric investigation of the interaction of GDH with rabbit anti-human GDH antibody.

作者信息

Carty P, O'Kennedy R, Lorenzo Abad E, Fernández Alvarez J M, Rodriguez Flores J, Smyth M R, Tipton K

机构信息

School of Biological Sciences, Dublin City University, Ireland.

出版信息

Analyst. 1990 May;115(5):617-21. doi: 10.1039/an9901500617.

DOI:10.1039/an9901500617

PMID:2396748

Abstract

A procedure for the isolation of glutamate dehydrogenase (GDH) from human liver, which involves the use of ion-exchange chromatography on diethylaminoethyl cellulose and affinity chromatography on guanosine triphosphate conjugated to Sepharose 4B, is described. The adsorptive voltammetric behaviour of human GDH, bovine GDH and rabbit anti-human GDH antibody was optimised with respect to accumulation potential, accumulation time and scan rate. The lower limits of detection were 0.2 and 1.2 mg l-1 for human and bovine GDH, respectively, and the lower limit of detection for rabbit anti-GDH antibody was 0.04 mg l-1. The interaction of human GDH with rabbit anti-human GDH antibody was also examined using this method.

摘要

描述了一种从人肝脏中分离谷氨酸脱氢酶（GDH）的方法，该方法包括在二乙氨基乙基纤维素上进行离子交换色谱以及在与琼脂糖凝胶4B偶联的三磷酸鸟苷上进行亲和色谱。针对富集电位、富集时间和扫描速率，优化了人GDH、牛GDH和兔抗人GDH抗体的吸附伏安行为。人GDH和牛GDH的检测下限分别为0.2和1.2 mg l-1，兔抗GDH抗体的检测下限为0.04 mg l-1。还使用该方法研究了人GDH与兔抗人GDH抗体的相互作用。