{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T10:56:11Z","timestamp":1758279371720},"reference-count":35,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2004,2,19]],"date-time":"2004-02-19T00:00:00Z","timestamp":1077148800000},"content-version":"vor","delay-in-days":9180,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Supramol Struct"],"published-print":{"date-parts":[[1979,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The surface of the HeLa cell is composed of a heterogeneous population of sialogly coproteins which undergo lectin\u2010mediated endocytosis (Kramer and Canellakis, Biochim Biophys Acta 551:328, 1979). One such sialoglyco\u2010protein, gamma protein, is the major periodate\u2010Schiff\u2010reactive and [<jats:sup>3<\/jats:sup>H]\u2010glucosamine\u2010labeled component of the plasma membrane; it has an apparent molecular weight of 165,000. Gamma protein is also the major [<jats:sup>125<\/jats:sup>I]\u2010wheat germ agglutinin\u2010binding component in sodium dodecyl sulfate gels. Neuraminidase digestion of HeLa cells abolishes binding of [<jats:sup>125<\/jats:sup>I]\u2010wheat germ agglutinin to gamma protein, and pretreatment of cells with wheat germ agglutinin protects gamma protein from desialation by neuraminidase. suggesting that wheat germ agglutinin binds to the sialic acid residues of gamma protein at the cell surface. Gamma protein can be extracted with various detergents but not with high\u2010salt, chelating, or chaotropic agents. Intact inside\u2010out plasma membrane vesicles have been prepared from HeLa cells that had phagocytosed latex particles. Treatment of these isolated vesicles with trypsin reduces the molecular weight of gamma protein. These results suggest that gamma protein is an integral membrane protein that spans the plasma membrane. Gamma protein can be purified to homogeneity by sequential lithium diiodosalicylate\u2010phenol extraction, wheat germ agglutinin\u2010agarose affinity chromatography, and preparative sodium dodecyl sulfate\u2010polyacrylamide gel electrophoresis.<\/jats:p>","DOI":"10.1002\/jss.400120404","type":"journal-article","created":{"date-parts":[[2005,5,28]],"date-time":"2005-05-28T05:38:49Z","timestamp":1117258729000},"page":"435-455","source":"Crossref","is-referenced-by-count":4,"title":["Isolation and properties of gamma protein, the major transmembrane sialoglycoprotein of the HeLa cell"],"prefix":"10.1002","volume":"12","author":[{"given":"Randall H.","family":"Kramer","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"E. 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