Immunochemical characterization of a human high molecular weight — melanoma associated antigen identified with monoclonal antibodies
dc.contributor.author | Ferrone, Soldano | en_US |
dc.contributor.author | Ruberto, Giovanna | en_US |
dc.contributor.author | Wilson, Barry S. | en_US |
dc.date.accessioned | 2006-09-11T18:16:53Z | |
dc.date.available | 2006-09-11T18:16:53Z | |
dc.date.issued | 1983-03 | en_US |
dc.identifier.citation | Wilson, Barry S.; Ruberto, Giovanna; Ferrone, Soldano; (1983). "Immunochemical characterization of a human high molecular weight — melanoma associated antigen identified with monoclonal antibodies." Cancer Immunology Immunotherapy 14(3): 196-201. <http://hdl.handle.net/2027.42/46851> | en_US |
dc.identifier.issn | 1432-0851 | en_US |
dc.identifier.issn | 0340-7004 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/46851 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6188530&dopt=citation | en_US |
dc.description.abstract | Sodium dodecyl sulfate polyacrylamide gel analysis of a high molecular weight (HMW) human melanoma associated antigen (MAA) defined by murine monoclonal antibodies revealed a number of distinct polypeptides ranging from 80,000 up to 280,000 daltons, in addition to an extremely heterogeneous group of components distributed over a wide range in apparent molecular weight (300,000–700,000 daltons). The 280,000 dalton and the larger heterogeneous molecular weight material are glycosylated since they are labeled with 3 H-sugars. The HMW-MAA is readily solubilized in the absence of detergents and the entire series of polypeptides fractionates together in the void volume of a Sephadex G200 column. Peptide maps of the various polypeptides of the HMW-MAA, generated by Staphylococcus aureus V-8 protease, are essentially the same except that some of the proteolytic fragments derived from the lower molecular weight polypeptides (80,000 daltons) are present in greater amounts than are similar fragments derived from the larger molecular weight polypeptides; the latter finding suggests that the complexity in molecular weight of the MAA may reflect combinations of several base subunits. Proteolytic cleavage of the HMW-MAA generates a number of peptides ranging in molecular weight from 77,000 daltons to less than 12,000 daltons, which still react with monoclonal antibodies and can distinguish monoclonal antibodies specific for different antigenic determinants of this MAA. | en_US |
dc.format.extent | 1563712 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Springer-Verlag; Springer-Verlag GmbH & Co KG | en_US |
dc.subject.other | Cancer Research | en_US |
dc.subject.other | Oncology | en_US |
dc.subject.other | Immunology | en_US |
dc.subject.other | Biomedicine | en_US |
dc.title | Immunochemical characterization of a human high molecular weight — melanoma associated antigen identified with monoclonal antibodies | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Microbiology and Immunology | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Pathology, University of Michigan Medical School, 1335 East Catherine Street, 48109, Ann Arbor, MI | en_US |
dc.contributor.affiliationum | Department of Pathology, University of Michigan Medical School, 1335 East Catherine Street, 48109, Ann Arbor, MI; Departments of Pathology and Surgery, College of Physicians and Surgeons of Columbia University, 10032, New York, NY, USA | en_US |
dc.contributor.affiliationother | Departments of Pathology and Surgery, College of Physicians and Surgeons of Columbia University, 10032, New York, NY, USA | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 6188530 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/46851/1/262_2004_Article_BF00205360.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF00205360 | en_US |
dc.identifier.source | Cancer Immunology Immunotherapy | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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