![]() |
|
|
Department of Physiology, University of California, Berkeley, California
Glucokinase activities were determined in 9 rat tissues liver, brain, muscle, kidney, small intestine, heart, spleen, adipose tissue and mammary gland. Significant amounts of glucokinase activity were particle-bound in brain (40 to 55%), in heart (50 to 60%) and in mammary gland (40%). In the other tissues, almost all of the activity appeared in the particle-free supernatant fraction. Except for a minor response by small intestine, liver was the only tissue in which glucokinase activity responded significantly to nutritional treatment of the rat. Evidence for the existence of 2 distinct enzymes capable of phosphorylating glucose was obtained from a study of the Km (glucose) values for the enzymes in the particle-free supernatant fraction of rat liver. The hepatic enzyme with a high Km value for glucose was shown to adapt to dietary treatment, whereas the hepatic glucokinase with a low Km for glucose was non-adaptable. Mannokinase activities were determined in brain, liver and mammary gland. The rates at which brain, liver and mammary gland phosphorylated mannose were 33, 27 and 26%, respectively, of those observed for glucose.
Manuscript received 8 February 1964.
This article has been cited by other articles:
![]() |
V. Douard and R. P. Ferraris Regulation of the fructose transporter GLUT5 in health and disease Am J Physiol Endocrinol Metab, August 1, 2008; 295(2): E227 - E237. [Abstract] [Full Text] [PDF] |
||||