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A radiochemical procedure for the assay of fatty acid binding by proteins

✍ Scribed by Jan F.C. Glatz; Jacques H. Veerkamp

Publisher: Elsevier Science
Year: 1983
Tongue: English
Weight: 593 KB
Volume: 132
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(83)90429-3

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✦ Synopsis

Protein-bound and unbound fatty acids can be efficiently separated at 0 degree C using a hydrophobic column-packing material (Lipidex 1000) similar to the separation of protein-bound and unbound steroids (E. Dahlberg, M. Snochowski, and J.-A. Gustafsson (1980) Anal Biochem. 106, 380-388). Protein-bound fatty acids are also removed by Lipidex 1000 when treatment is performed at 37 degrees C. Lipidex 1000 does not exhibit binding properties for soluble proteins at 0 and 37 degrees C, in contrast to dextran-coated charcoal. Lipidex 1000 appeared to be useful for the delipidation of protein samples at 37 degrees C and for a radiochemical assay of fatty acid-binding by microgram amounts of protein at 0 degree C. With this assay we obtained results on palmitate binding to serum albumin similar to those reported on the basis of equilibrium dialysis. Delipidated proteins from dealbuminized rat liver cytosol maximally bind about 4 nmol palmitate/mg protein.

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