{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,19]],"date-time":"2026-01-19T00:36:55Z","timestamp":1768783015297,"version":"3.49.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1970,4,1]]},"abstract":"<jats:p>1. The Barrett (1967) assay for cathepsin D was slightly modified. 2. The enzyme was purified from liver of man and chicken by a procedure involving autolysis, acetone fractionation, ion-exchange chromatography and isoelectric focusing. 3. Several isoenzymes of cathepsin D were resolved in the isoelectric-focusing step, and three major forms, \u03b1,\u03b2 and \u03b3, were distinguished for each species. 4. A modified analytical method of isoelectric focusing in polyacrylamide gel indicated a high degree of homogeneity of the purified \u03b2 and \u03b3 isoenzymes from each species, and this was supported by their constant high specific activities. 5. Gel filtration of the isoenzymes in a calibrated column of Sephadex G-100 showed that each had a molecular weight of 45000. 6. Human cathepsin D had a pH optimum of 3.5, and that of chicken enzyme was 3.0, haemoglobin being used as substrate. In each species, the three isoenzymes have the same pH-dependence curve. 7. The purified cathepsin D samples showed very little action on acid-denatured albumin.<\/jats:p>","DOI":"10.1042\/bj1170601","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T19:27:27Z","timestamp":1439234847000},"page":"601-607","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":191,"title":["Cathepsin D. Purification of isoenzymes from human and chicken liver"],"prefix":"10.1042","volume":"117","author":[{"given":"A. J.","family":"Barrett","sequence":"first","affiliation":[{"name":"Tissue Physiology Department, Strangeways Research Laboratory, Cambridge CB1 4RN, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/117\/3\/601\/766930\/bj1170601.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/117\/3\/601\/766930\/bj1170601.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T19:07:24Z","timestamp":1637953644000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/117\/3\/601\/17136\/Cathepsin-D-Purification-of-isoenzymes-from-human"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1970,4,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1970,4,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1170601","relation":{},"ISSN":["0306-3283"],"issn-type":[{"value":"0306-3283","type":"print"}],"subject":[],"published":{"date-parts":[[1970,4,1]]}}}