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Fig. 4. (A) Distinct species of ß1 chain on the cell surface. Lanes 1-4: K562 were surface labelled with different antibodies to ß1 integrin (lane 1, control; 2, B3B11; 3, JB1A; 4, 12G10) and washed to remove free antibodies. The cells were lysed and the antibody-associated integrins were immunoprecipitated, separated by SDS-PAGE and immunoblotted with JB1A to detect total ß1. Lanes 5-7: total cell lysates from untreated cells were prepared and incubated with antibodies for immunoprecipitation (lanes 5, B3B11; 6, JB1A; 7, 12G10). The samples were analysed as described above. Note that the patterns of capture are different for the surface-labelled and the cell lysate-derived integrins demonstrating the specificity of the cell surface capture. Lanes 8-10: cells were grown in serum-free medium and surface labelled with 12G10, lane 8; 12G10 in the presence of 120 kDa fragment of fibronectin, lane 9; or surface labelled with 12G10, washed and exposed to the 120 kDa fragment of fibronectin, lane 10. The bound integrins were isolated by immunoprecipitation and processed as described above. (B) Lack of association between 5 and the 12G10 reactive ß1 subunits. Cell surface integrins were immunoprecipitated with antibodies to 5 with JBS5 or to ß1, with B3B11, JB1A or 12G10. The precipitates were separated by SDS-PAGE and probed by western blot analysis with anti-ß1, JB1A (upper panel) or a polyclonal anti-5 (lower panel).

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