{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,16]],"date-time":"2025-10-16T20:26:03Z","timestamp":1760646363389},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1982,10,15]]},"abstract":"<jats:p>A protein with pore-forming activity has been isolated from the outer membrane of rat liver mitochondria. The purification involves sucrose gradient centrifugation, differential centrifugation in the presence of Triton X-100, and DEAE-Sepharose and CM-Sepharose chromatography. The yield of the purified protein was approx. 2% of the total outer membrane proteins. The protein, when inserted into soya bean phospholipid vesicles, increases the [3H]sucrose permeability of the vesicles but had no effect on the permeability of high-molecular-weight [14C]dextran (Mr 70 000). The protein is very active, since as little as 3-4 micrograms of protein per mg of phospholipid is required for the complete release of [3H]sucrose from the vesicles. Sucrose diffusion channels could not be reconstituted with other membrane proteins such as rat liver cytochrome oxidase or cytochrome b5. Purified pore protein revealed a single band of apparent Mr 30000 when resolved by sodium dodecyl sulphate\/polyacrylamide-gel electrophoresis. This polypeptide could be further resolved by isoelectric focusing into a major (pI7.9) and two relatively minor (pI7.6 and 7.2) components. Proteolytic mapping with V8 proteinase from Staphylococcus aureus suggests that these probably represent a single component showing charge heterogeneity. The reason for the charge heterogeneity is not known. The amino acid composition of the protein revealed 47.8% polar amino acids with a relatively high lysine content.<\/jats:p>","DOI":"10.1042\/bj2080077","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:34:54Z","timestamp":1439238894000},"page":"77-82","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":76,"title":["Purification of a protein having pore forming activity from the rat liver mitochondrial outer membrane"],"prefix":"10.1042","volume":"208","author":[{"given":"M","family":"Lind\u00e9n","sequence":"first","affiliation":[]},{"given":"P","family":"Gellerfors","sequence":"additional","affiliation":[]},{"given":"B D","family":"Nelson","sequence":"additional","affiliation":[]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/208\/1\/77\/625855\/bj2080077.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/208\/1\/77\/625855\/bj2080077.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T12:59:37Z","timestamp":1637845177000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/208\/1\/77\/14391\/Purification-of-a-protein-having-pore-forming"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1982,10,15]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1982,10,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2080077","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1982,10,15]]}}}