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Purine Pathway Enzyme Abnormalities in Acute Lymphoblastic Leukemia¹

Leukemia Biology Section, Pediatric Oncology Branch, National Cancer Institute, Bethesda, Maryland 20205 [D. G. P., J. B.], and Department of Hematology-Oncology, Children's Hospital National Medical Center, Washington, D. C. 20010 [G. R.]

The status of three purine pathway enzymes, adenosine deaminase, 5'-nucleotidase, and purine nucleoside phosphorylase, was evaluated in the leukemic cells of patients with acute lymphoblastic leukemia and correlated with routine immunological cell surface markers. A distinct pattern of enzyme activity was noted in T-lymphoblasts which have significantly higher adenosine deaminase activity (p < 0.02) and lower 5'-nucleotidase (p < 0.001) and purine nucleoside phosphorylase (p < 0.01) activities than do non-T, non-B lymphoblasts. This enzyme pattern is similar to that observed in normal human thymocytes but is not shared by the mature, normal T-lymphocytes of peripheral blood, suggesting that it may reflect the differentiation status of malignant T-lymphoblasts. These findings, which confirm the biochemical heterogeneity of acute lymphoblastic leukemia, may provide an avenue for selective chemotherapy of this disease.

¹ Presented at the Conference on Cell Markers in Acute Leukemia, March 4 and 5, 1980, Bethesda, Md.

² To whom reprints for requests should be addressed, at Pediatric Oncology Branch, National Cancer Institute, Building 10, Room 3B03, NIH, Bethesda, Md. 20205.

³ Special Fellow of the Leukemia Society of America.