{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T16:22:57Z","timestamp":1762100577669},"reference-count":35,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T00:00:00Z","timestamp":1160006400000},"content-version":"vor","delay-in-days":10353,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Neurochemistry"],"published-print":{"date-parts":[[1978,6]]},"abstract":"<jats:p><jats:bold>Abstract\u2014<\/jats:bold> \u03b3\u2010Glutamyl transpeptidase from bovine choroid plexus has been shown to be a membrane\u2010bound enzyme. Partial purification of the enzyme has been accomplished using detergent extraction and ammonium sulfate fractionation. Important determinants of enzymatic activity with acceptor substrates included chain length, stereoisomerism, and amino acid composition of the acceptors. L\u2010Methionine was the best amino acid substrate and its corresponding peptides L\u2010methionylmethionine and L\u2010methionyl\u2010L\u2010serine were also good \u03b3\u2010glutamyl acceptors. L\u2010Alanine and glycine were poor acceptor substrates; whereas, some peptides containing these amino acids were excellent substrates. Glycylglycine was significantly more effective as a \u03b3\u2010glutamyl acceptor than glycine, triglycine, or tetraglycine. L\u2010Alanylglycine was a superior acceptor to glycine, L\u2010alanine, or L\u2010alanylglycylglycine, while the D\u2010isomer of alanylglycine was only minimally effective as an acceptor substrate. In general glycyl peptides were the best acceptor substrates examined. Our findings that \u03b3\u2010glutamyl transpeptidase could catalyze the transfer of \u03b3\u2010glutamyl groups to glycylglycyl\u2010L\u2010alanine and L\u2010alanylglycylglycine are of special interest, since few examples of tripeptide acceptors for the enzyme have been found. It is suggested that \u03b3\u2010glutamyl transpeptidase might play a role in the inactivation and\/or transport of biologically active peptides.<\/jats:p>","DOI":"10.1111\/j.1471-4159.1978.tb10453.x","type":"journal-article","created":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T08:01:27Z","timestamp":1160035287000},"page":"1253-1259","source":"Crossref","is-referenced-by-count":13,"title":["PARTIAL PURIFICATION AND KINETICS OF \u03b3\u2010GLUTAMYL TRANSPEPTIDASE FROM BOVINE CHOROID PLEXUS"],"prefix":"10.1111","volume":"30","author":[{"given":"Paul E.","family":"Prusiner","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stanley B.","family":"Prusiner","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2006,10,5]]},"reference":[{"key":"e_1_2_2_2_1","first-page":"312","volume":"25","author":"Albert Z.","year":"1966","journal-title":"Acta Histochem. 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