[Partial purification and study of gamma-glutamyl transpeptidase from sheep cerebral capillaries].
Gamma-glutamyl transpeptidase was purified 53 times from Sheep brain cortex capillaries. On gel filtration it appears homogeneous with a M.W. = 350 000. The enzyme is likely a glycoprotein, the properties of which are close to hog kidney gamma-glutamyl transpeptidase ; gamma-glutamyl aminoacid formation is assayed electrophoretically. The results obtained using several aminoacids are in favour of the existence of different units, specific of each group of aminoacids ; together with the data from structural analogs, they support the hypothesis that gamma-glutamyl transpeptidase participates in aminoacid transport accross blood brain barrier.
D000596:Amino Acids / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D001693:Biological Transport, Active; D001812:Blood-Brain Barrier; D002196:Capillaries / Q000201:enzymology*; D002540:Cerebral Cortex / Q000098:blood supply*; D008970:Molecular Weight; D012756:Sheep; D014364:Tryptophan / Q000031:analogs & derivatives / Q000378:metabolism; D005723:gamma-Glutamyltransferase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism
D000596:Amino Acids; D014364:Tryptophan; D005723:gamma-Glutamyltransferase
Purification partielle et étude de la gamma-glutamyl transpeptidase des capillaires cérébraux de mouton