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Summary  Glycerol kinase was measured by a modification of the radiochemical enzyme test described by Newsholme and coworkers in isolated epididymal and parametrial fat cells and liver tissue of obese hyperglycaemic Bar Harbor mice (obob) and their lean littermates (ob+ob+). The specific activity of glycerol kinase was independent of age in the control animals. It was about 90 times greater in liver than in fat cells. In obese animals glycerol kinase was dependent on age. Compared with the controls, the activity was significantly increased in fat cells of 2–12-month old mice and in liver of 5-month old mice. In fat cells of 2–12-month old mice fedad libitum, glycerol kinase activity was significantly correlated to serum IRI-levels. — Glycerol kinase activity decreased during fasting or experimental insulin deficiency, induced by streptozotocin. It was significantly increased in fat cells and liver by insulin substitution. This insulin effect was suppressed by actinomycin D. — It is concluded that insulin regulates glycerol kinase activity by enzyme induction. — The significance of these results for the adipose tissue metabolism in obob mice is discussed.

Regulation of glycerol kinase by insulin in isolated fat cells and liver of Bar Harbor Obese Mice