Abstract
The binding of [1- 14C]oleate to rat liver cytosol was studied, using gel filtration on Sephadex G-75 and G-50. In liver cytosols from control rats, most of the high-affinity oleate binding was in the region of 12 000-dalton proteins. In liver cytosols from diabetic and starved rats, a second peak of radioactivity appeared in the void volume. This peak was shown to be associated with a component having the molecular weight of 400 000. Evidence suggesting that a change in the composition of cytosolic binding proteins is involved is presented.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
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