Abstract
A fatty acid binding protein has been purified from etiolated Avena sativa seedlings. The successive steps of purification comprised heat denaturation (50°C), (NH 4) 2SO 4 fractionation, gel filtration on Sephacryl S-200, CM-chromatography, and preparative isoelectric focusing. The homogeneity of the protein was ascertained by electrophoretic titration and SDS-polyacrylamide gel electrophoresis. The protein has an isoelectric point of 8.4 and an apparent molecular weight of 8700 ± 500. The purified protein is capable of binding long-chain fatty acids and their CoA-esters. A high affinity ( K d 3.5 · 10 −6 M) of oleic acid for the basic protein was found by independent measurements of association and dissociation kinetics.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
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