{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,3]],"date-time":"2026-04-03T14:26:51Z","timestamp":1775226411285,"version":"3.50.1"},"reference-count":32,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T00:00:00Z","timestamp":1160006400000},"content-version":"vor","delay-in-days":9927,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Neurochemistry"],"published-print":{"date-parts":[[1979,8]]},"abstract":"<jats:p><jats:bold>Abstract\u2014<\/jats:bold> An enzyme with the specificity of a prolyl endopeptidase was purified about 880\u2010fold from rabbit brain. The enzyme hydrolyzes peptidylprolyl\u2010peptide and peptidylprolyl\u2010amino acid bonds. Several biologically active peptides such as angiotensin, bradykinin, neurotensin. substance P and thyrotropin releasing hormone are degraded by hydrolysis of the bond between the carboxyl group of proline and the adjacent amino acid or ammonia respectively. The enzyme is activated by dithiothreitol and inhibited by heavy metals and thiol blocking agents. The serine protease inhibitor phenylmethanesulfonylfluoride has no effect on activity; however, inhibition was obtained with diisopropylfluorophosphate. Prolyl endopeptidase has a molecular weight of about 66,000 and a pH optimum of about 8.3. A new chromogenic substrate, <jats:italic>N<\/jats:italic>\u2010benzyloxycarbonylglycyl\u2010L\u2010prolylsulfamethoxazole, was used for determination of enzyme activity. The substrate is hydrolyzed to <jats:italic>N<\/jats:italic>\u2010benzyloxycarbonylglycyl\u2010L\u2010proline and free sulfamethoxazole which can be conveniently determined by a colorimetric procedure.<\/jats:p>","DOI":"10.1111\/j.1471-4159.1979.tb05176.x","type":"journal-article","created":{"date-parts":[[2006,10,5]],"date-time":"2006-10-05T09:53:29Z","timestamp":1160042009000},"page":"461-469","source":"Crossref","is-referenced-by-count":145,"title":["PURIFICATION AND PROPERTIES OF A PROLYL ENDOPEPTIDASE FROM RABBIT BRAIN"],"prefix":"10.1111","volume":"33","author":[{"given":"Marian","family":"Orlowski","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elizabeth","family":"Wilk","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stevens","family":"Pearce","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sherwin","family":"Wilk","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","doi-asserted-by":"publisher","DOI":"10.1042\/bj0910222"},{"key":"e_1_2_2_3_1","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/S0021-9258(18)73708-3","article-title":"A new coupling component for sulfanilamide determination","volume":"128","author":"Brayton A. 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