Quantitative analysis of cell surface HLA structures by means of monoclonal antibodies.

Quantitative data on the binding of murine monoclonal antibodies ot whole human lymphoblastoid lines and peripheral blood lymphocytes (PBL) are reported. Antibodies reacting with beta 2m or a common part of the HLA heavy chains and nonpolymorphic determinants of the DR dimer were used. The equilibrium constant (K) of the reaction and the total number of antigenic determinants was graphically estimated. For the above-mentioned antibodies, K ranged between 5 X 10(8) and 4 C 10(9) l/mole at 0 degrees C and progressively decreased with the increasing temperature. T cells expressed less HLA and beta 2M determinants than the B cells. The number of determinants per surface unit is higher on the B cell from PBL than on E.B. virus-transformed cell lines and is generally very low, suggesting that the complement-dependent cytotoxic activity is a phenomenon depending on membrane fluidity. A portion of beta 2m seems not to be bound to the HLA heavy chains on B cells as well as on T line surface, as already shown for Molt 4 line.