Reactivity of fluorodinitrobenzene with intact human leucocytes: Examination of sites of action and the molecular entities involved in interaction.

The epsilon amino groups of lysine and to a lesser extent amino groups on phosphotidyl ethanolamine and phosphotidyl serine situated on cell membranes of normal human leucocytes have been identified as the sites of dinitrophenylation. In situ conversion of 10,000 hydrophylic amino sites into hydrophobic sites on cell surfaces causes conformational changes in cell membranes with exposures of leukaemic cell-specific neo-antigens on tagged cell surfaces.

Nature of leukemia-associated antigenicity of dinitrophenylated human lymphocytes and lymphoblasts.

Using dinitrophenylated human lymphocytes and phytohaemagglutinin–stimulated human lymphoblasts as antigens, antibodies were produced in rabbits. The immunological reactivities of the antisera so produced were tested against various types of leukemic cells after absorbing the sera with pooled normal leukocytes. Both the sera showed reactivity with all types of leukemic cells and no specific affinity for lymphoid leukemic cells was seen. This may suggest the presence of some common antigens on all types of leukemic cells or that dinitrophenylation brings about similar changes on all types of normal leukocytes.