Correlations between enzymatic and immunologic properties of human peripheral blood mononuclear cells. I. Ectoenzymes of normal and immunodeficient peripheral blood mononuclear cells.

The activity of plasma membrane marker enzymes which are involved in purine metabolism (5'-nucleotidase, alkaline 5'-nucleotide phosphodiesterase), in active ion transport (Na-K-Mg-adenosine triphosphatase, ouabain-sensitive Na-K-adenosine triphosphatase), in aminoacid transport (gamma-glutamyltranspeptidase), and in basic physiologic functions (alkaline phosphomonoesterase) were assayed in mononuclear cells isolated from peripheral blood of normal donors and of patients with primary immunodeficiency. Irrespective of the clinical classification of the immunodeficiency, the cells of patients were characterized by significantly diminished 5'-nucleotidase and to a certain extent by lower alkaline phosphomonoesterase activities. Average activity levels of other enzymes were similar in cells of patients and controls, but scattering was more pronounced in the first group. Determination of substrate affinity revealed different kinetic properties of 5'-nucleotidase in cells from patients and normal donors; however, the extent of inhibition by beta-glycerophosphate or alpha, beta-adenosine-methylene diphosphate was comparable for both types of cells. The presence of inhibitory compounds in patients' serum was excluded by mixing experiments. When activities of the various plasma-membrane-associated enzymes were compared with each other, significant correlations emerged in normal lymphocytes. Most of these correlations were absent in cell membranes of immunodeficient patients. The findings indicate that the plasma membrane of lymphocytes from patients with immunodeficiency may be characterized by an altered distribution of enzymatic constituents.