Modification of the Adipocyte Lipid Binding Protein by Sulfhydryl

the modification of ALBP with NEM nor the addition of oleic acid had a significant effect on protein ... romercuri)benzenesulfonic acid, and Sephadex ...
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7408

Biochemistry 1990, 29, 7408-7413

Modification of the Adipocyte Lipid Binding Protein by Sulfhydryl Reagents and Analysis of the Fatty Acid Binding Domain+ Melissa K. Buelt and David A. Bernlohr* Department of Biochemistry, University of Minnesota, St. Paul, Minnesota 55108 Received October 23, 1989; Revised Manuscript Received March 26, 1990

ABSTRACT: The adipocyte lipid binding protein (ALBP) is a member of a multigene family of low molecular weight proteins which stoichiometrically and saturably bind hydrophobic ligands and presumably facilitate intracellular lipid metabolism. To probe the structure-function relationship of the binding domain of ALBP, chemical modification has been employed. Modification of the two cysteinyl residues of ALBP (Cys' and Cys'I7) with a variety of sulfhydryl reagents decreased the apparent affinity for oleic acid in the following order of effectiveness: methyl methanethiosulfonate