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Enzymes of Glycogen Metabolism in White Blood Cells

I. Glycogen Phosphorylase in Normal and Leukemic Human Leukocytes^*

Adel A. Yunis and Grace K. Arimura

( Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri)

Glycogen phosphorylase has been assayed in normal leukocytes and in those obtained from patients with chronic granulocytic and chronic lymphocytic leukemia. Assay was performed in the direction of both glycogen degradation and glycogen synthesis with and without adenylic acid. The results indicate that (a) a major portion of phosphorylase activity exists in the active or a form as evidenced by 30–70 per cent activity in the absence of adenosine-5'-phosphate, (b) wide variations in activity were noted in leukocytes from different donors, (c) leukocyte phosphorylase activity in leukemic cells did not differ significantly from the normal. Some of the properties of leukocyte glycogen phosphorylase and its relation to phosphorylase from liver and muscle are discussed.

^* Supported by grants from U. S. Public Health Service #CA 06213-02, HE 00022-17; by American Cancer Society Institutional Research Grant to Washington University #IN36D; and by gifts in memory of Philipp Hunkel, Mark Edison, Bill Burns, and Joe Blanchard.

Leukemia Society, Inc., Scholar.

Received 10/ 7/63.