Abstract
Four independent monoclonal antibodies derived from spleen cells of rats immunized with mouse NIH/3T3 cells were found to precipitate an 80,000-dalton plasma membrane glycoprotein, identified as a polymorphic differentiation antigen of murine mesenchymal cells. The homology of the four immunoprecipitated polypeptides was proven by analysis of partial proteolytic cleavage products. The genetic polymorphism detected by the four antibodies was shown to reside in a single antigenic site by several criteria: (i) The expression of the antigenic determinant among different strains of mice; (ii) cross-inhibition of antibody binding; (iii) precipitation of partial proteolytic cleavage fragments of the 80,000-dalton glycoprotein; (iv) the kinetics of heat inactivation. These antibodies thus define a single polymorphic site of a major phagocytic cell surface glycoprotein and provide the basis for genetic and functional characterization of this glycoprotein.
Original language | English (US) |
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Pages (from-to) | 718-722 |
Number of pages | 5 |
Journal | Archives of Biochemistry and Biophysics |
Volume | 209 |
Issue number | 2 |
DOIs | |
State | Published - Jul 1981 |
Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology