Biochemical characterization of a T-lymphoma-specific 90,000 molecular weight disulfide linked dimeric glycoprotein

Details

Serval ID
serval:BIB_B791598AF92C
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Biochemical characterization of a T-lymphoma-specific 90,000 molecular weight disulfide linked dimeric glycoprotein
Journal
Molecular Immunology
Author(s)
Spiazzi  A., Corradin  G., Nagasawa  R., Tridente  G., MacDonald  H. R., Bron  C.
ISSN
0161-5890 (Print)
Publication state
Published
Issued date
07/1987
Volume
24
Number
7
Pages
719-27
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jul
Abstract
The biochemical features of a membrane antigen detected by a mouse monoclonal antibody (A1) raised against the murine thymoma cell line EL4 are described. This reagent detected a novel disulfide-linked 90,000 mol. wt dimeric membrane glycoprotein composed of two chains of approx 45,000 mol. wt. Endo-beta-N-acetylglucosaminidase F digestion generated a single 28,000 polypeptide, thus suggesting that the A1 molecule is a homodimer. No structural homology between the A1 molecule and the human T 90/44 protein (9.3 antigen) could be revealed by peptide mapping analysis. In view of the fact that three polypeptides of mol. wts 28,000-30,000, 21,000 and 15,000 respectively co-precipitated with the A1 antigen, the possible relationship of the A1 molecular complex to other known T-cell surface antigens including the antigen receptor is discussed.
Keywords
Animals Antigens, Neoplasm/*analysis Antigens, Surface/*analysis Cell Line Chemistry Electrophoresis, Polyacrylamide Gel Membrane Glycoproteins/*analysis/immunology Mice Mice, Inbred BALB C Molecular Weight Peptide Mapping Thymoma/*immunology Thymus Neoplasms/*immunology
Pubmed
Web of science
Create date
24/01/2008 14:55
Last modification date
20/08/2019 15:25
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