PMID: 6104563Jan 1, 1980Paper

Structural, functional, and clinical aspects of gamma-glutamyltransferase

CRC Critical Reviews in Clinical Laboratory Sciences
D M Goldberg

Abstract

GGT catalyses the transfer of gamma-glutamyl residues to amino acids or small peptides. A number of publications report the purification of GGT, the rat kidney enzyme being the best characterized. Bromelain treatment liberates an active form with a molecular weight of 68,000 separable into two nonidentical glycopeptides with molecular weights of 46,000 and 22,000; the latter contains the gamma-glutamyl binding site. GGT is intimately concerned in the synthesis and metabolism of glutathione through the gamma-glutamyl cycle. There is good evidence that this plays a role in the absorption of amino acids from the glomerular filtrate and from the intestinal lumen through a translocation mechanism. Many studies indicate that the GGT content of liver is increased by enzyme-inducing drugs and that this increase is reflected in elevated activity of the enzyme in blood serum. The serum assay has potential in monitoring drug compliance. Increased serum GGT activity encountered in chronic alcoholics seems to be partly due to microsomal enzyme induction. Utility of the assay in detecting alcoholism is controversial, but it is a useful index to compliance with therapy. Dramatic increases in activity are found in many chemically-induced anima...Continue Reading

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