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Fatty acid binding protein: stimulation of microsomal phosphatidic acid formation.
Results demonstrate for the first time that both L-F ABP and I-FABP stimulate liver microsomal phosphatidic acid formation by enhancing synthesis of phosphatidate from fatty acyl-CoA and glycerol 3-phosphate.
Acyl-CoA binding proteins: Multiplicity and function
The identity, nature, function, and pathobiology of these fascinating newly discovered long-chain fatty acyl-CoA binding proteins are explored.
The role of aromatic side chain residues in micelle binding by pancreatic colipase. Fluorescence studies of the porcine and equine proteins.
The emission maximum of horse colipase at 345 nm indicates a solvent-accessible tryptophan residue which becomes less so on binding of micelles, and the data are consistent with a direct insertion of dansyl-NH-tyrosine-55 into the micelle.
Physical-chemical studies on the role of the metal ions in concanavalin A.
Time-dependent changes in the intrinsic cotton effects of concanavalin A.
The spectroscopic effects observed in the near W CD which are associated with binding of metals at both sites S1 and S2, (ii) Ca’+-induced time dependence and (iii) binding of a-methyl-D-mannoside are all modulated by a symmetrical, broad 277 nm transition.
Recombinant liver fatty acid binding protein interacts with fatty acyl-coenzyme A.
In this study, highly pure recombinant L-FABP and I-F ABP were used first to establish binding to fatty acyl-CoAs and then to examine the effects of these FABPs on microsomal phosphatidic acid synthesis.
The spectrum of cobalt bovine procarboxypeptidase A, an index of catalytic function.
Abstract The spectra of functionally essential, chromophoric metal atoms of metalloenzymes are thought to reflect catalytic potential [Vallee and Williams (1968) Proc. Nat. Acad. Sci. USA 59, 498].