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Evidence for phosphorylation of pancreatic islet pyruvate kinase
Authors:M J MacDonald  A Kowluru  C M Chang
Affiliation:University of Wisconsin Medical School, Madison USA.
Abstract:
Rabbit pancreatic islet cytosol catalyzes the calcium-activated phosphorylation by [gamma 32P]ATP of a protein with a molecular weight of 57,000 that is precipitated with antipyruvate kinase antibodies. We were unable to demonstrate that phosphorylation in the presence of calcium or cAMP had any immediate effect on rat pancreatic islet pyruvate kinase activity. This finding is consistent with our inability to confirm the finding of others that pancreatic islets contain phosphoenolpyruvate carboxykinase activity (Diabetes, 34:246, 1985). Since the carboxykinase catalyzes phosphoenolpyruvate formation and pyruvate kinase catalyzes essentially the opposite reaction, if the carboxykinase were present in the beta cell, pyruvate kinase would need to be inhibited to prevent recycling of phosphoenolpyruvate.
Keywords:Address reprint requests to Michael J. MacDonald   University of Wisconsin Medical School   1300 University Ave   Room 3459   Madison   WI 53706.
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