Fluorescence analysis study of the lability of biomembranes and their components. III. Kinetics of complex formation between bovine serum albumin molecules and higher saturated fatty acids

• Published in: Biofizika Vol. 21; no. 1; p. 75
• Main Authors: Orlov, S N, Rebrov, V G, Malkov, Iu A, Fedin, V A, Danilov, V S
• Format: Journal Article
• Language: Russian
• Published: Russia (Federation) 01-01-1976
• Subjects: Fatty Acids; Serum Albumin, Bovine; Spectrometry, Fluorescence
• ISSN: 0006-3029

Kinetic peculiarities of the sorption of natural limited fatty acids on the molecules of bovine serum albumine (BSA) were studied by investigating fluorescent parameters of ionic (1-anilinonaphtalin-8-sulphonate-ANS) and neutral (N-phenyl-1-naphtylamine-PNA) probes. The following regularities were found: 1. The parameters which characterize the microsurroundings of both probes (quantum yield of fluorescence, the binding constant) did not change significantly during the sorption of the fattyn acids (laurinic, palmitinic and methyl ether of the stearinic acid). An exponential character of BSA fluorescent titration with fatty acids points to a competitive character of the relationship dye -- fatty acid for the binding sites in hydrophobic sacks of BSA. 2. The study of the character of the effect of solution ionic strength on the sorption of fatty acids showed that along with hydrophobic interactions the electrostatic interaction between carboxyl residues of fatty acids and charged protein groups also significantly contributed to this process. 3. Temperature relationship of AMS and PNA fluorescence intensity in the complex BSA -- laurinic acid correlates well with temperature relationship obtained from a pure protein system.