{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T21:54:21Z","timestamp":1773266061184,"version":"3.50.1"},"reference-count":0,"publisher":"Canadian Science Publishing","issue":"10","license":[{"start":{"date-parts":[[1982,10,1]],"date-time":"1982-10-01T00:00:00Z","timestamp":402278400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.nrcresearchpress.com\/page\/about\/CorporateTextAndDataMining"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Can. J. Biochem."],"published-print":{"date-parts":[[1982,10,1]]},"abstract":"<jats:p> We have determined optimal conditions for the solubilization of the basic somatomedin (SM) receptor from human plancental membranes and for the measurement of the binding of basic SM to the solubilized receptor. Further, we have developed conditions under which the basic SM receptor, in the presence of equivalent amounts of insulin receptor, can be selectively and specifically affinity-labeled with <jats:sup>125<\/jats:sup>I-labeled basic SM, using the cross-linking reagent disuccinimidyl suberate (DSS). Our results with these developed methods indicate that the properties of the soluble basic SM receptor (pH optimum for ligand binding, pH 7 to 9; adsorption to lectin-agarose derivatives; sedimentation coefficient in detergent\u2013sucrose solutions, 11S) closely parallel data previously reported for the insulin receptor. Based on the sedimentation coefficient and the previously estimated Stokes radius of the soluble receptor (7.2\u2002nm), a molecular weight of 402\u2002000 can be calculated for the detergent\u2013receptor complex. Electrophoretic analysis of the basic SM receptor, selectively cross-linked to <jats:sup>125<\/jats:sup>I-labeled basic SM with DSS in the presence of excess unlabeled insulin revealed, under reducing conditions, a major labeled constituent of 140 kdaltons, substantiating our previous work employing a photoaffinity labeling reagent. DSS cross-linking also demonstrated the presence of less intensely labeled components with apparent molecular weights of 54\u2002000, 43\u2002000 and 35\u2002000 but failed to reveal a distinct 90- to 100-kdalton species visualized in parallel experiments with insulin. The 53-kdalton species was not detected in similar experiments with insulin. A specifically labeled basic SM receptor component of 300 kdaltons was also observed under reducing conditions; in the absence of \u03b2-mercaptoethanol, all labeled components migrated in the 300-kdalton range. In comparison, selective DSS labeling of the insulin receptor in the presence of excess basic SM revealed components which, upon electrophoresis under reducing conditions, exhibited apparent molecular weights of 300\u2002000, 140\u2002000, 90\u2002000\u2013100\u2002000, 43\u2002000 and 35\u2002000. The major insulin-labeled component (140\u2002000) comigrated with the major constituent (140\u2002000) selectively labeled with basic SM. Chymotryptic digestion of the receptors selectively DSS labeled with either <jats:sup>125<\/jats:sup>I-labeled insulin or <jats:sup>125<\/jats:sup>I-labeled basic SM yielded quite similar, but distinctive, gel electrophoretic maps. We conclude that the receptors for basic SM and insulin are highly homologous structures, particularly with respect to their glycoprotein nature, their hydrodynamic properties, their disulphide cross-linked composition, and with respect to the size of the major constituent detected by selective affinity labeling. Nonetheless, the detection of electrophoretically distinct labeled receptor substituents upon analysis of specifically labeled material, both before and after chymotryptic cleavage, points to subtle differences between the polypeptide compositions of the two receptors. <\/jats:p>","DOI":"10.1139\/o82-119","type":"journal-article","created":{"date-parts":[[2009,12,21]],"date-time":"2009-12-21T14:58:49Z","timestamp":1261407529000},"page":"923-932","source":"Crossref","is-referenced-by-count":17,"title":["Characterization of the human placental receptor for basic somatomedin"],"prefix":"10.1139","volume":"60","author":[{"given":"B.","family":"Bhaumick","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G. D.","family":"Armstrong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M. D.","family":"Hollenberg","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R. M.","family":"Bala","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"155","container-title":["Canadian Journal of Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nrcresearchpress.com\/doi\/pdf\/10.1139\/o82-119","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,1,5]],"date-time":"2020-01-05T22:57:05Z","timestamp":1578265025000},"score":1,"resource":{"primary":{"URL":"http:\/\/www.nrcresearchpress.com\/doi\/10.1139\/o82-119"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1982,10,1]]},"references-count":0,"journal-issue":{"issue":"10","published-print":{"date-parts":[[1982,10,1]]}},"alternative-id":["10.1139\/o82-119"],"URL":"https:\/\/doi.org\/10.1139\/o82-119","relation":{},"ISSN":["0008-4018"],"issn-type":[{"value":"0008-4018","type":"print"}],"subject":[],"published":{"date-parts":[[1982,10,1]]}}}