Studies on the insulin mediator. II. Separation of two antagonistic biologically active materials from fraction II.
Insulin treatment significantly altered the elution profile of deproteinized muscle extracts chromatographed on Sephadex G-25 columns, particularly in fraction II, which contains the insulin mediator. Further purification of fraction II by high-voltage paper electrophoresis at pH 1.9 and 3.5 resulted in two active fractions. Fraction 1 leads to 4 stimulated the cyclic AMP-dependent protein kinase and inhibited glycogen synthase phosphoprotein phosphatase, and may be a novel substance. Fractions 1 leads to 6 and 3 leads to 6 inhibited the cyclic AMP-dependent protein kinase and stimulated glycogen synthase phosphatase. It is proposed that the insulin mediator is present in fractions 1 leads to 6 and 3 leads to 6.
D000818:Animals; D002850:Chromatography, Gel; D000242:Cyclic AMP / Q000494:pharmacology; D004789:Enzyme Activation; D006007:Glycogen-Synthase-D Phosphatase / Q000378:metabolism; D007295:Inositol Phosphates; D007700:Kinetics; D009132:Muscles / Q000032:analysis*; D011134:Polysaccharides; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D011972:Receptor, Insulin / Q000302:isolation & purification* / Q000378:metabolism
D007295:Inositol Phosphates; D011134:Polysaccharides; C028039:inositol phosphate glycan; D000242:Cyclic AMP; D011494:Protein Kinases; D011972:Receptor, Insulin; D006007:Glycogen-Synthase-D Phosphatase