Characterization of a porcine genomic clone encoding a major histocompatibility antigen: expression in mouse L cells.
- 1 March 1982
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 79 (5), 1403-1407
- https://doi.org/10.1073/pnas.79.5.1403
Abstract
A porcine genomic clone encoding a major histocompatibility (MHC) antigen was isolated by direct screening of a swine genomic library with a heterologous human MHC c[complementary]DNA probe. Mouse L cells transformed with DNA from the clone stably express swine MHC antigen. Pig alloantisera specifically lyse transformant but not control cell lines in a complement-mediated cytotoxicity assay. Direct immunoprecipitation of radiolabeled cellular protein from transformant lines by pig alloantiserum results in the coprecipitation of swine MHC H chain and mouse .beta.2-microglobulin, demonstrating the association of heterologous subunits of MHC antigens.This publication has 34 references indexed in Scilit:
- A pseudogene homologous to mouse transplantation antigens: Transplantation antigens are encoded by eight exons that correlate with protein domainsCell, 1981
- Multiple sequences related to classical histocompatibility antigens in the mouse genomeNature, 1981
- Three cDNA clones encoding mouse transplantation antigens: Homology to immunoglobulin genesCell, 1981
- The Major Histocompatibility Complex of the MouseScience, 1979
- The isolation of structural genes from libraries of eucaryotic DNACell, 1978
- High resolution two-dimensional electrophoresis of basic as well as acidic proteinsCell, 1977
- Analysis of H-2 and Ia molecules by two-dimensional gel electrophoresis.The Journal of Experimental Medicine, 1977
- Molecular similarities between the Qa-2 alloantigen and other gene products of the 17th chromosome of the mouse.The Journal of Experimental Medicine, 1977
- TRANSPLANTATION IN MINIATURE SWINETransplantation, 1976
- Detection of specific sequences among DNA fragments separated by gel electrophoresisJournal of Molecular Biology, 1975