|
|
||||||||
From the Department of Biology and the Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
Abstract
A cell surface glycoprotein (designated T100) of apparent m.w. 100,000 by SDS-PAGE under reducing and non-reducing conditions was precipitated from NP-40 extracts of surface radiolabeled thymocytes from a variety of inbred strains of mice by the standard noncongenic Lyt-2.1-typing serum. The inbred strain distribution, trypsin sensitivity on intact cells, and apparent m.w. of T100 suggest that it is different from Lyt-2.1. Inheritance and expression of T100 suggest that it is determined by an allele at a single genetic locus, and testing of CXB recombinant inbred strains and B6.C minor histocompatibility congenic strains suggest that this locus is linked to H-25. Antiserum absorption experiments, two-stage cytotoxicity assays, and results of immunoprecipitations performed after prebinding antibody to radio-labeled thymocytes suggest that some T100 is accessible to antibody on the intact cell surface. However, for unknown reasons the number of cells required to absorb anti-T100 precipitating activity from antiserum was much higher than for removal of anti-Lyt-2.1 activity. A molecule with properties of T100 was also detected on lymph node cells and on the AKTB-1 lymphoma.
Footnotes
1 This work was supported by United States Public Health Service Research Grant CA 15808 from the National Cancer Institute to P.D.G. and by United States Public Health Service Research Grant CA 14051 from the National Cancer Institute to the Massachusetts Institute of Technology Center for Cancer Research.
2 Postdoctoral Fellow of the Charles A. King Trust, Boston, Massachusetts. Portions of these studies were performed under a postdoctoral fellowship from the Leukemia Society of America.
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |