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dc.contributor.authorCanfield, Ann E
dc.contributor.authorSchor, Ana M
dc.contributor.authorWest, David C
dc.contributor.authorSchor, Seth L
dc.contributor.authorGrant, M E
dc.date.accessioned2010-10-20T11:49:10Z
dc.date.available2010-10-20T11:49:10Z
dc.date.issued1987-08-15
dc.identifier.citationIdentification and partial characterization of two major proteins of Mr 47,000 synthesized by bovine retinal endothelial cells in culture. 1987, 246 (1):121-9 Biochem. J.en
dc.identifier.issn0264-6021
dc.identifier.pmid3675551
dc.identifier.urihttp://hdl.handle.net/10541/113551
dc.description.abstractBiosynthetic experiments with cultured bovine retinal endothelial cells have identified a glycoprotein of Mr 47,000 (Gp47) as a major component secreted into the medium. Gp47 is a non-collagenous glycoprotein with a pI of 4.6-5.5, which does not bind to either gelatin-Sepharose or heparin-Sepharose but is retained by concanavalin A-Sepharose. The Mr of this species decreases to approx. 42,000 in the presence of tunicamycin, indicating that it contains asparagine-linked oligosaccharides. A second protein of Mr 47,000 (P47) is present in the cell layer/matrix of these cultured cells. The electrophoretic mobility of P47 remains unaltered when synthesized in the presence of tunicamycin. Peptide-mapping experiments using N-chlorosuccinimide and Staphylococcus aureus V8 proteinase demonstrate that Gp47 and P47 are distinct proteins, and are not related to colligin, a membrane-bound collagen-receptor protein of similar size, or to SPARC, a major secreted product of parietal endodermal cells and sparse cultures of aortic endothelial cells.
dc.language.isoenen
dc.subject.meshAnimals
dc.subject.meshCattle
dc.subject.meshCells, Cultured
dc.subject.meshChromatography, Affinity
dc.subject.meshElectrophoresis, Polyacrylamide Gel
dc.subject.meshEndothelium
dc.subject.meshEye Proteins
dc.subject.meshIsoelectric Focusing
dc.subject.meshMolecular Weight
dc.subject.meshPeptide Mapping
dc.subject.meshRetina
dc.titleIdentification and partial characterization of two major proteins of Mr 47,000 synthesized by bovine retinal endothelial cells in culture.en
dc.typeArticleen
dc.contributor.departmentDepartment of Biochemistry and Molecular Biology, School of Biological Sciences, University of Manchester, U.K.en
dc.identifier.journalBiochemical Journalen
html.description.abstractBiosynthetic experiments with cultured bovine retinal endothelial cells have identified a glycoprotein of Mr 47,000 (Gp47) as a major component secreted into the medium. Gp47 is a non-collagenous glycoprotein with a pI of 4.6-5.5, which does not bind to either gelatin-Sepharose or heparin-Sepharose but is retained by concanavalin A-Sepharose. The Mr of this species decreases to approx. 42,000 in the presence of tunicamycin, indicating that it contains asparagine-linked oligosaccharides. A second protein of Mr 47,000 (P47) is present in the cell layer/matrix of these cultured cells. The electrophoretic mobility of P47 remains unaltered when synthesized in the presence of tunicamycin. Peptide-mapping experiments using N-chlorosuccinimide and Staphylococcus aureus V8 proteinase demonstrate that Gp47 and P47 are distinct proteins, and are not related to colligin, a membrane-bound collagen-receptor protein of similar size, or to SPARC, a major secreted product of parietal endodermal cells and sparse cultures of aortic endothelial cells.


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