ANOMERIC SPECIFICITY OF HEXOKINASE IN RAT, HUMAN, AND MURINE TUMOR-CELLS

  • 1 January 1985
    • journal article
    • research article
    • Vol. 45  (12) , 6376-6378
Abstract
In tumoral cells derived from the insulin-producing rat cell line RINm5F, both low- and high-Km glucose-phosphorylating enzymic activities were present. The hexokinase-like enzyme was inhibited by glucose 6-phosphate and displayed a greater affinity for but lower maximal velocity with .alpha.-D-glucose than .beta.-D-glucose. A comparable anomeric behavior of hexokinase was observed in breast cancer (MCF-7) and lymphocytic leukemia (P388) cells. Thus, the anomeric specificity of hexokinase in tumoral cells was not different from that recently characterized in normal mammalian cells.

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