PMID: 6102743Feb 1, 1980

Isolation and purification of multiple forms of gamma-glutamyl transpeptidase from rat brain

Neurochemical Research
E Reyes, T D Barela

Abstract

Four different forms of the enzyme gamma-glutamyl transpeptidase were isolated from rat brain by chromatography on concanavalin A. An approximate 1500-fold purification was achieved. The four forms were characterized with respect to molecular weight, Km for gamma-glutamyl-p-nitroanilide, mobility on polyacrylamide gels, and inhibitory effects of borate-serine. The multiple forms of the enzyme were found to have molecular weights ranging from 74,000 to 234,000 and Kms of 0.07 to 8.6 mM. It was determined that in brain, the major portion of the enzyme activity is associated with plasma membrane fragments and endoplasmic reticulum.

References

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Citations

May 23, 2000·Journal of Neuroscience Research·F V MenaH R Zielke
Aug 11, 1981·Molecular and Cellular Biochemistry·E K MichaelisD R Kuonen
Jun 15, 1982·Experientia·R A WapnirL A Goldstein
Mar 15, 1991·Clinica Chimica Acta; International Journal of Clinical Chemistry·A R SajjanK S Datta
Jan 1, 1984·International Journal of Developmental Neuroscience : the Official Journal of the International Society for Developmental Neuroscience·M Pajari
Jul 6, 2000·Progress in Neurobiology·R Dringen
Feb 11, 1986·Nucleic Acids Research·J Coloma, H C Pitot
Aug 15, 1989·European Journal of Biochemistry·A PapandrikopoulouH G Gassen
Jul 1, 1990·Journal of Neurochemistry·M YudkoffI Nissim
Jul 1, 1984·Neurochemical Research·J Veselý, M Cernoch
Oct 1, 1985·Neurochemical Research·J VeselýM Cernoch
Jan 1, 1992·Critical Reviews in Toxicology·T J Monks, S S Lau

Related Concepts

Ammonium Sulfate
Brain
Molecular Sieve Chromatography
SDS-PAGE
Gamma-glutamyl transferase

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