{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T11:18:48Z","timestamp":1758280728408},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1987,3,15]]},"abstract":"<jats:p>Covalent cross-linking techniques have been used to investigate the structural characteristics of the growth-hormone (GH) receptor in a variety of rabbit liver cell membrane preparations (particulate and soluble). Two classes of GH-binding protein have been identified which differ in their Mr by gel filtration and susceptibility to precipitation with poly(ethylene glycol) (PEG). The first, a PEG-precipitable (Mr approximately 300,000) protein, contained Mr-65,000 and Mr-40,000 binding proteins linked by disulphide bonds. It was present in aqueous extracts derived from microsomal membranes but was not present in cytosol preparations. The second, a PEG-non-precipitable protein (Mr approximately 100,000) was composed of a non-disulphide-linked primary GH-binding subunit of Mr 60,000-66,000. This binding protein was present in all rabbit liver cell fractions and\/or preparations. Both binding-protein classes contained intramolecular disulphide bonds. It is not clear whether the Mr-approximately 100,000 form, or perhaps higher-Mr species which have not been identified by cross-linking studies, represents the native, endogenous, form of the GH receptor present in particulate microsomal or plasma membranes. Accordingly, although these data have identified two classes of GH-binding protein, especially a primary GH-binding subunit of Mr 60,000-66,000, they indicate that, unlike studies on the insulin receptor, covalent cross-linking techniques alone are not sufficient to delineate the complete subunit structure of the native and endogenous form of the GH receptor.<\/jats:p>","DOI":"10.1042\/bj2420713","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:57:48Z","timestamp":1439240268000},"page":"713-720","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":11,"title":["Structural studies on membrane-bound and soluble growth-hormone-binding proteins of rabbit liver"],"prefix":"10.1042","volume":"242","author":[{"given":"S I","family":"Ymer","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A C","family":"Herington","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/242\/3\/713\/590547\/bj2420713.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/242\/3\/713\/590547\/bj2420713.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T18:19:14Z","timestamp":1637864354000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/242\/3\/713\/25352\/Structural-studies-on-membrane-bound-and-soluble"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1987,3,15]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1987,3,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2420713","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1987,3,15]]}}}