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Solubilization of the H-2 antigen from hybrid cells of mouse mammary ascites tumor and mouse L cells at high cell concentrations in detergent.

Radioiodinated membrane components of L-FM3ANo.2 cells, which were hybrid cells of C3H/He mouse mammary ascites tumor and mouse L cells, were solubilized with non-ionic detergent Nonidet P-40 and immunoprecipitated with anti-H-2k sera. The immune complexes were reduced and subjected to SDS-polyacrylamide gel electrophoresis. When the cells were lysed at a concentration of 2 X 10(7) cells/ml in 0.5% NP-40 buffer, only H-2 molecules including beta2-microglobulin were precipitated, but when the cells were lysed at a concentration of 8 X 10(7) cells/ml in 0.5% NP-40 buffer, two labeled components corresponding to molecules of 105,000 daltons and 85,000 daltons, respectively, were observed in addition to the characteristic radioactive peaks of the H-2 antigen. Dilution of the latter detergent lysate with phosphate buffered saline exhibited no effect on the detection of the two additional components, while further treatment of the lysate with NP-40 buffer abrogated them to be detected. The results indicate that the H-2 molecules were solubilized as physical complexes with certain membrane components of L-FM3ANo.2 cells when the cells were lysed at high cell concentrations in detergent, and suggest that the H-2 molecules and certain membrane components may be physically associated with each other on the cell surface of L-FM3ANo.2 cells.