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Characterization of purine nucleoside phosphorylase in leukemia
Author(s) -
Morisaki Takayuki,
Horiuchi Naomi,
Fujii Hisaichi,
Miwa Shiro
Publication year - 1986
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.2830230310
Subject(s) - purine nucleoside phosphorylase , purine metabolism , inosine , leukemia , purine , enzyme , chronic lymphocytic leukemia , peripheral blood mononuclear cell , myeloid leukemia , chemistry , deoxyguanosine , biochemistry , microbiology and biotechnology , biology , cancer research , immunology , dna , in vitro
Purine nucleoside phosphorylase (PNP) activity was determined in mononuclear cells from 49 patients with various types of leukemia. A low level of PNP activity was found in mononuclear cells from patients with acute myeloid and lymphoblastic leukemia and with chronic lymphocytic leukemia. Enzymatic and immunological studies on PNP from leukemic cells of these patients revealed no differences in Michaelis constant for inosine, thermostability, electrophoretic mobility, immunological reactivity, or specific activity between the PNP of leukemic cells and that of normal mononuclear cells. These results suggest that the decrease in PNP activity of leukemic cells is due to a decreased rate of enzyme synthesis. Thus, the abnormality of PNP activity might be due to an alteration in the regulatory mechanism of enzyme synthesis in the purine metabolism in the leukemic clone.