Journal Article


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



animals cattle immunology humans glutamate dehydrogenase liver rabbits antigen antibody reactions isolation purification enzymology

Purification of human glutamate dehydrogenase (GDH) and an adsorptive voltammetric investigation of the interaction of GDH with rabbit anti-human GDH antibody. (1990)

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.
Collections Ireland -> Dublin City University -> PubMed

Full list of authors on original publication

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

Experts in our system

R O'Kennedy
Dublin City University
Total Publications: 211