{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,6]],"date-time":"2026-03-06T07:04:38Z","timestamp":1772780678916,"version":"3.50.1"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1975,12,1]]},"abstract":"<jats:p>1. The polypedtide chains that comprise the subunits of the tonofilaments, or the \u03b1-keratin component, of bovine epidermis were fractionated by combination of chromatography on DEAE-cellulose and preparative polyacrylamide-gel electrophoresis. 2. The seve polypeptide chains investigated had generalyy similar properties; all contained two residues per molecule of tryptophan and N-acetylserine was the common N-terminal amino acid residue. 3. On the basis of close similarities in \u03b1-helix content and amino acid composition, the polypeptide chains were classified into three distinct groups. Each group contained approximately one-third of the total polypeptides on a molar basis. The groups and designated polypeptides chain numbers were: group one, polypeptides 1a and 1b, which had moleculae weights of 58,000, contained about 25% \u03b1-helix, 86 glutamic acid and 8 cysteine residues per molecule, but which differed in net charge, extinction coefficients and tyrosine contents; group two, polypeptides 2, 3, and 4, which hadmolecular weights within thewithin the range of 52,00-56,000, contained about 48% \u03b1-helix, 54 glutamic acid and 6 cysteine residues per molecule, but which differed in extinction coefficients and tryosine contents; and group, polypeptides 5 and 6, which had molecular weights of 47000-48000, contained about 56% \u03b1-helix, 64 glutamic acid and 4 cysteine residues per molecule, but which differed in extinction coefficients and tyrosine contents, it is suggested that none of the chains is a precursor or a degradation product of other polypeptidc chains. 5. It is concluded that bovine epidermal \u03b1-keratin consists of a heterogeneous group of similar polypeptide chains.<\/jats:p>","DOI":"10.1042\/bj1510603","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:00:10Z","timestamp":1439236810000},"page":"603-614","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":105,"title":["The polypeptide composition of bovine epidermal \u03b1-keratin"],"prefix":"10.1042","volume":"151","author":[{"given":"P M","family":"Steinert","sequence":"first","affiliation":[{"name":"Dermatology Branch, National Cancer Institute, Bethesda, Md. 20014, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"W W","family":"Idler","sequence":"additional","affiliation":[{"name":"Dermatology Branch, National Cancer Institute, Bethesda, Md. 20014, U.S.A."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/151\/3\/603\/566495\/bj1510603.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/151\/3\/603\/566495\/bj1510603.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T16:53:47Z","timestamp":1637945627000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/151\/3\/603\/9989\/The-polypeptide-composition-of-bovine-epidermal"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1975,12,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1975,12,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1510603","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1975,12,1]]}}}