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This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Smythe, J Articles by Anstee, D. Search for Related Content PubMed PubMed Citation Articles by Smythe, J Articles by Anstee, D. Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Quantitation of the number of molecules of glycophorins C and D on normal red blood cells using radioiodinated Fab fragments of monoclonal antibodies J Smythe, B Gardner and DJ Anstee International Blood Group Reference Laboratory, Bristol, UK. Two rat monoclonal antibodies (BRAC 1 and BRAC 11) have been produced. BRAC 1 recognizes an epitope common to the human erythrocyte membrane glycoproteins glycophorin C (GPC) and glycophorin D (GPD). BRAC 11 is specific for GPC. Fab fragments of these antibodies and BRIC 10, a murine monoclonal anti-GPC, were radioiodinated and used in quantitative binding assays to measure the number of GPC and GPD molecules on normal erythrocytes. Fab fragments of BRAC 11 and BRIC 10 gave values of 143,000 molecules GPC per red blood cell (RBC). Fab fragments of BRAC 1 gave 225,000 molecules of GPC and GPD per RBC. These results indicate that GPC and GPD together are sufficiently abundant to provide membrane attachment sites for all of the protein 4.1 in normal RBCs. Volume 83, Issue 6, pp. 1668-1672, 03/15/1994 Copyright © 1994 by The American Society of Hematology CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: R. F. Workman and P. S. Low Biochemical Analysis of Potential Sites for Protein 4.1-mediated Anchoring of the Spectrin-Actin Skeleton to the Erythrocyte Membrane J. Biol. Chem., March 13, 1998; 273(11): 6171 - 6176. [Abstract] [Full Text] [PDF] S. M. Marfatia, J. H. Morais-Cabral, A. C. Kim, O. Byron, and A. H. Chishti The PDZ Domain of Human Erythrocyte p55 Mediates Its Binding to the Cytoplasmic Carboxyl Terminus of Glycophorin C. ANALYSIS OF THE BINDING INTERFACE BY IN VITRO MUTAGENESIS J. Biol. Chem., September 26, 1997; 272(39): 24191 - 24197. [Abstract] [Full Text] [PDF] N. J. Hemming, D. J. Anstee, M. A. Staricoff, M. J. A. Tanner, and N. Mohandas Identification of the Membrane Attachment Sites for Protein 4.1 in the Human Erythrocyte J. Biol. Chem., March 10, 1995; 270(10): 5360 - 5366. [Abstract] [Full Text] [PDF]

	Copyright © 1994 by American Society of Hematology         Online ISSN: 1528-0020