{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T07:07:02Z","timestamp":1762067222869},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1977,6,1]]},"abstract":"<jats:p>Three large fragments of human serum albumin were produced by peptic digestion of the native protein [Geisow &amp; Beaven (1977) Biochem. J. 161, 619-625]. Fragment P44 represents residues 1-386 and fragments P29 and P31 represent residues 49-307 and residues 308-584 respectively of the albumin molecule. The large N-terminal fragment P44 has a similar percentage of alpha-helix to stored defatted albumin, although the alpha-helix content of all the fragments is significantly less than that of freshly prepared albumin. The fragment P44 appears to account for all the binding of the hydrophobic probe 8-anilinonaphthalene-1-sulphonate to albumin. N-Acetyl-L-tryptophan binds to this fragment and displaces one of the bound molecules of 8-anilinonaphthalene-1-sulphonate. Bilirubin binds to fragments P44 and P29, and the complexes show similar circular-dichroism spectra to that of the complex between bilirubin and whole albumin. These results are in agreement with affinity-labeling work on albumin with reactive ligands where substitution occurs in the N-terminal region of the molecule. The sharp conformational transitional transition in albumin which is observed between pH4 and 3.5 was absent from the fragments. This isomerization, usually called the N-F transition, probably occurs in intact albumin as a result of the unfolding or separation of the C-terminal third of the protein from the remainder of the molecule.<\/jats:p>","DOI":"10.1042\/bj1630477","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:06:31Z","timestamp":1439237191000},"page":"477-484","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":54,"title":["Physical and binding properties of large fragments of human serum albumin"],"prefix":"10.1042","volume":"163","author":[{"given":"M J","family":"Geisow","sequence":"first","affiliation":[]},{"given":"G H","family":"Beaven","sequence":"additional","affiliation":[]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/163\/3\/477\/568925\/bj1630477.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/163\/3\/477\/568925\/bj1630477.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T17:38:39Z","timestamp":1637948319000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/163\/3\/477\/11336\/Physical-and-binding-properties-of-large-fragments"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1977,6,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1977,6,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1630477","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1977,6,1]]}}}