{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T07:07:05Z","timestamp":1762067225285},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"5","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1968,8,1]]},"abstract":"<jats:p>1. [32P]Lecithin and [32P]phosphatidylethanolamine were prepared by incubating rat liver mince with [32P]phosphate. With these 32P-labelled phospholipids conditions for the quantitative assay of phospholipase A activity were established. 2. The distribution of phospholipase A activity between subcellular fractions of the bovine adrenal medulla was determined. Phospholipases A1 and A2, with pH optima at 4\u00b72 and 6\u00b75 respectively, were found in the large-granule fraction. By means of sucrose-density-gradient centrifugation it was shown that both these phospholipases were localized in lysosomes. 3. Lysosomal phospholipase A1 catalysed the hydrolysis of [32P]lecithin and [32P]phosphatidylethanolamine at the same rate. The enzymic activity was inhibited by 70% in the presence of 10mm-calcium chloride. 4. Lysosomal phospholipase A2 catalysed the hydrolysis of [32P]phosphatidylethanolamine more rapidly than it hydrolysed [32P]lecithin. The hydrolysis of [32P]phosphatidylethanolamine, but not that of [32P]lecithin, by phospholipase A2 was activated by 0\u00b78mm-calcium chloride. However, the hydrolysis of both substrates was inhibited by 8mm-calcium chloride. 5. The significance of the presence of phospholipase activity in lysosomes is discussed in relation to the functions of lysosomes in general and in the adrenal medulla.<\/jats:p>","DOI":"10.1042\/bj1080867","type":"journal-article","created":{"date-parts":[[2015,8,13]],"date-time":"2015-08-13T21:36:44Z","timestamp":1439501804000},"page":"867-874","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":66,"title":["Lysosomal phospholipases A1 and A2 of bovine adrenal medulla"],"prefix":"10.1042","volume":"108","author":[{"given":"A D","family":"Smith","sequence":"first","affiliation":[{"name":"Department of Pharmacology, University of Oxford"}]},{"given":"H","family":"Winkler","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, University of Oxford"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/108\/5\/867\/761286\/bj1080867.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/108\/5\/867\/761286\/bj1080867.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,29]],"date-time":"2021-11-29T20:55:22Z","timestamp":1638219322000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/108\/5\/867\/3492\/Lysosomal-phospholipases-A1-and-A2-of-bovine"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1968,8,1]]},"references-count":0,"journal-issue":{"issue":"5","published-print":{"date-parts":[[1968,8,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1080867","relation":{},"ISSN":["0306-3283"],"issn-type":[{"value":"0306-3283","type":"print"}],"subject":[],"published":{"date-parts":[[1968,8,1]]}}}