Anomeric specificity of hexokinase in rat, human, and murine tumor cells.
نویسندگان
چکیده
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.
منابع مشابه
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عنوان ژورنال:
- Cancer research
دوره 45 12 Pt 1 شماره
صفحات -
تاریخ انتشار 1985