Document Detail

Structure of the murine plasma cell alloantigen PC-1: comparison with the receptor for transferrin.
MedLine Citation:
PMID:  6292294     Owner:  NLM     Status:  MEDLINE    
The plasma cell alloantigen PC-1 was isolated from C1.18 myeloma cells by immunoprecipitation and was analyzed by polyacrylamide gel electrophoresis. It was found to consist of two similar or identical disulfide-bonded polypeptide chains, each of Mr 115,000. The mobility of PC-1 in nonequilibrium pH gradient electrophoresis was similar to that of bovine serum albumin (pI 4.9). The PC-1 antigen is therefore similar to the transferrin receptor in Mr, charge, subunit composition, disulfide bonding, and developmental regulation. Similarities can also be detected by peptide mapping with subtilisin, but not with staphylococcal V8 protease. It is suggested that the PC-1 protein and the transferrin receptor may have had a common evolutionary origin, and may have similar functions.
J W Goding; F W Shen
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of immunology (Baltimore, Md. : 1950)     Volume:  129     ISSN:  0022-1767     ISO Abbreviation:  J. Immunol.     Publication Date:  1982 Dec 
Date Detail:
Created Date:  1983-01-07     Completed Date:  1983-01-07     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985117R     Medline TA:  J Immunol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2636-40     Citation Subset:  AIM; IM    
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MeSH Terms
Antigens, Surface / analysis,  immunology*
Glycoproteins / immunology
Isoelectric Point
Macromolecular Substances
Molecular Weight
Plasma Cells / immunology*
Receptors, Cell Surface / immunology
Receptors, Transferrin
Grant Support
Reg. No./Substance:
0/Antigens, Surface; 0/Glycoproteins; 0/Macromolecular Substances; 0/Receptors, Cell Surface; 0/Receptors, Transferrin; 11096-37-0/Transferrin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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