PHOSPHOFRUCTOKINASE IN HUMAN-BLOOD CELLS

  • 1 January 1979
    • journal article
    • research article
    • Vol. 54  (2) , 389-400
Abstract
The subunit composition of phosphofructokinase from normal and malignant blood cells was investigated by immunologic, electrophoretic and chromatographic methods. Immunoprecipitation tests were performed with 3 specific antisera recognizing each of the basic subunits of human phosphofructokinase: muscle, M-type; liver, L-type and fibroblast, F-type. Mature polymorphonuclear cells contain mainly L-subunits, while lymphocytes and platelets contain hybrids formed of L and F subunits; these hybrids can be electrophoretically separated. Red cell phosphofructokinase is composed of L and M subunits as judged by its reactivity with anti-L and anti-M type antisera. The various M-L hybrids composing red cell phosphofructokinase could only be separated by chromatography on DEAE-cellulose. Lymphocytes from patients with chronic lymphocytic leukemia and lymphoblasts from patients with acute lymphoblastic leukemia contain phosphofructokinase forms similar to those from normal lymphocytes, while the immature granulocytic cells (leukemic myeloblasts and myeloid cells of chronic myeloid leukemia) are characterized by a reinforcement of enzyme inhibition by anti-F-type antiserum. Lymphoid lines in culture (Epstein-Barr virus (EBV)-induced or malignant lymphoma-derived lines) are characterized by the indistinctive expression of all 3 basic subunits, similar to that found in some fetal tissues. This is the 1st description of the isozymic nature of phosphofructokinase in platelets and white blood cells and of its changes with malignancy and cell culture. This enzyme may represent a useful marker in the characterization of the leukemic cells. and of its changes with malignancy and cell culture. This enzyme may represent a useful marker in the.