PURIFICATION OF HUMAN GLUTAMATE-DEHYDROGENASE (GDH) AND AN ADSORPTIVE VOLTAMMETRIC INVESTIGATION OF THE INTERACTION OF GDH WITH RABBIT ANTI-HUMAN GDH ANTIBODY

被引：6

作者：

CARTY, P

OKENNEDY, R

ABAD, EL

ALVAREZ, JMF

FLORES, JR

SMYTH, MR

TIPTON, K

机构：

[1] DUBLIN CITY UNIV,SCH CHEM SCI,DUBLIN 9,IRELAND

[2] DUBLIN CITY UNIV,SCH BIOL SCI,DUBLIN 9,IRELAND

[3] UNIV DUBLIN TRINITY COLL,DEPT BIOCHEM,DUBLIN 2,IRELAND

来源：

ANALYST | 1990年 / 115卷 / 05期

关键词：

Adsorptive stripping voltammetry; Anti-glutamate dehydrogenase antibody; Glutamate dehydrogenase;

D O I：

10.1039/an9901500617

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

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.

引用

页码：617 / 621

页数：5

共 18 条

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BEGERMAYER HU, 1974, METHOD ENZYMAT AN, V2, P650

[2]

BOYER PD, 1975, ENZYMES, P322

[3] PRODUCTION, PURIFICATION AND CHARACTERIZATION OF POLYCLONAL ANTIBODIES TO GLUTAMATE-DEHYDROGENASE FROM HUMAN LIVER [J].