In vitro study of γ-glutamyl transpeptidase in rat lens

γ-Glutamyl transpeptidase catalyzes the initial step in the utilization of glutathione. In the lens, this enzyme is accessible to externally supplied substrates. An efflux of glutathione from the lens occurs when it was incubated in saline. Inhibition of γ-glutamyl-transpeptidase by l-serine-borate...

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Veröffentlicht in:	Experimental eye research 1983-09, Vol.37 (3), p.273-278
Hauptverfasser:	Said, R., Bonne, C., Regnault, F., Sincholle, D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Biological and medical sciences cataract Eye and associated structures. Visual pathways and centers. Vision Fundamental and applied biological sciences. Psychology gamma -glutamyltransferase gamma-Glutamyltransferase - antagonists & inhibitors gamma-Glutamyltransferase - metabolism Glutamate-Cysteine Ligase - antagonists & inhibitors Glutamates - pharmacology Glutamine - analogs & derivatives glutathione Glutathione - metabolism Glutathione - pharmacology lens Lens, Crystalline - enzymology Methionine Sulfoximine - pharmacology Rats Rats, Inbred Strains Serine - pharmacology Vertebrates: nervous system and sense organs γ-glytamyl transpeptidase
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Beschreibung
Zusammenfassung:	γ-Glutamyl transpeptidase catalyzes the initial step in the utilization of glutathione. In the lens, this enzyme is accessible to externally supplied substrates. An efflux of glutathione from the lens occurs when it was incubated in saline. Inhibition of γ-glutamyl-transpeptidase by l-serine-borate decreases the rate of glutathione breakdown in the external medium and the rate of its decline in the lens.
ISSN:	0014-4835 1096-0007
DOI:	10.1016/0014-4835(83)90162-8