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Research shows that the stability of bovine beta-lactoglobulins against unfolding is markedly affected by the medium pH with both A and B variants of the protein stabilizing against urea and sodium dodesylsulfate denaturations at acidic and alkaline pH, respectively. Furthermore, complex formation of the variant B with oleic and palmitic acid is different from that of apoprotein and occurs at neutral pH.

Results demonstrate that the chicken liver basic fatty acid-binding protein is significantly different from the mammalian liver fatty acid-binding protein in terms of its relative affinity for different fatty acids and the number of bound ligands. Furthermore, chicken protein shows some similarity to catfish liver fatty acid-binding protein.

An investigation on the presence of partly folded states in solution was conducted to understand the mechanism of chicken liver bile acid-binding protein interaction with membranes. It was founded that L-BABP was partly unfolded at pH 2.5 and low ionic strength, retaining some of its secondary structure.

The X-ray structure of the cocrystals of chicken Lb-FABP completed with cholate is investigated and a reasonable endogenous ligand for a liver protein is presented. The results presented is of interest as a model for binding of cholate to these recognized bile acid transporters and examines the hypothesis that the Lb-FABPs may be more accurately described as bile acid-binding proteins rather than fatty acid-binding proteins.

Research has been conducted on fatty acid-binding proteins. The authors describe the toad liver fatty acid-binding protein's complete amino acid sequence, its ligand-binding properties, X-ray structure and fatty acid transfer mechanism to phospholipid membranes.