Genetic characterization of a polymorphic murine cell-surface glycoprotein

✍ Scribed by Jayne Lesley; Ian S. Trowbridge

• Publisher: Springer-Verlag
• Year: 1982
• Tongue: English
• Weight: 472 KB
• Volume: 15
• Category: Article
• ISSN: 0093-7711
• DOI: 10.1007/bf00364339

✦ Synopsis

As described in the preceding paper, monoclonal antibodies have been raised by immunization of rats with mouse hematopoietic cells which detect a maj or cell-surface glycoprotein (Mr = 95 000) of mouse bone-marrow cells of the granulocytic series. While most of the monoclonal antibodies detect this molecule on bone-marrow and spleen cells of all mouse strains, two antibodies recognize alternative allelic forms of the molecule. One alloantigen is expressed in all the remaining inbred strains examined. The alloantigens are codominantly expressed on the cells of F 1 mice. Backcrosses of DBA/2 and C57BL/6 with F1 mice (B6D2 F1) confirmed that a single genetic locus is involved in the expression of the two antigenic forms and demonstrated linkage to Ly-ml 1 which has previously been mapped to mouse chromosome 2. These genetic mapping experiments and the biochemical properties of the glycoprotein suggested that it might be identical to a glycoprotein first identified on murine fibroblasts by Hughes and August and designated Pgp-1. This has been firmly established by exchange of monoclonal antibody reagents and sequential immunoprecipitations.