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- W1509608128 abstract "Extracts of lymphocytes from normal donors and from patients with chronic lymphocytic leukemia (CLL) and acute lymphoblastic leukemia were examined for a variety of enzymes with activity for purine nucleotide biosynthesis, interconversion, and catabolism as well as for a selected number of enzymes involved in pyrimidine nucleotide metabolism. Lymphocytes from all three donor types (normal, CLL, acute lymphocytic leukemia) contained the following enzymatic activities: adenine and guanine phosphoribosyltransferase, adenosine kinase, nucleoside diphosphate kinase, adenylate kinase, guanylate kinase, cytidylate kinase, uridylate kinase, adenosine deaminase, purine nucleoside phosphorylase, and adenylate deaminase (with ATP). In contrast, no adenine deaminase, guanine deaminase, or xanthine oxidase activity could be demonstrated. Deoxycytidine deaminase was found in the lymphocytes from all the CLL patients but was not detected in the lymphocytes from the normal donors. The enzymes necessary for the de novo synthesis of purines were absent in lymphocytes from both normal donors and patients with CLL. The activity of all enzymes were quantitatively the same for the normal and CLL cells but severalfold higher activities were found for enzymes present in lymphoblasts from patients with acute lymphocytic leukemia.A related study involving the murine leukemic cells L5178Y and L1210 and the murine ascites Sarcoma 180 cells showed similar enzymatic patterns but with excessively elevated activities in comparison to lymphocytes from normal donors or from patients with CLL or acute lymphoblastic leukemia." @default.
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- W1509608128 date "1973-01-01" @default.
- W1509608128 modified "2023-09-23" @default.
- W1509608128 title "Identification of the enzymatic pathways of nucleotide metabolism in human lymphocytes and leukemia cells." @default.
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