Isolation and Purification of Multiple Forms of Gamma-glutamyl Transpeptidase from Rat Brain
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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.
Hemmings S, Storey K Mol Cell Biochem. 2000; 202(1-2):119-30.
PMID: 10706002 DOI: 10.1023/a:1007069431615.
Dringen R, Kranich O, Hamprecht B Neurochem Res. 1997; 22(6):727-33.
PMID: 9178957 DOI: 10.1023/a:1027310328310.
Solubilization and some properties of gamma-glutamyltransferase from human brain microvessels.
Vesely J, CERNOCH M Neurochem Res. 1984; 9(7):927-34.
PMID: 6150450 DOI: 10.1007/BF00964524.
Studies of gamma-glutamyltransferase activity in the brain tissue post mortem.
Vesely J, CERNOCH M Neurochem Res. 1984; 9(7):917-25.
PMID: 6150449 DOI: 10.1007/BF00964523.
Comparative ontogenesis of gamma-glutamyl transpeptidase in rat tissues.
Wapnir R, Mancusi V, Goldstein L Experientia. 1982; 38(6):647-8.
PMID: 6125405 DOI: 10.1007/BF01964069.