Intra-albumin migration of bound fatty acid probed by spin label ESR
- Department of Research and Development, MedInnovation GmbH, Berlin 13599 (Germany)
- Department of Environmental Medicine, International Sakharov Environmental University, Minsk 220009 (Belarus)
Conventional ESR spectra of 16-doxyl-stearic acid bound to bovine and human serum albumin were recorded at different temperatures in order to investigate the status of spin-labeled fatty acid in the interior of the protein globule. A computer spectrum simulation of measured spectra, performed by non-linear least-squares fits, clearly showed two components corresponding to strongly and weakly immobilized fatty acid molecules. The two-component model was verified on spectra measured at different pH. Thermodynamic parameters of the spin probe exchange between two spin probe states were analyzed. It was concluded that at physiological conditions, fatty acid molecules permanently migrate in the globule interior between the specific binding sites and a space among albumin domains.
- OSTI ID:
- 20991525
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 360, Issue 4; Other Information: DOI: 10.1016/j.bbrc.2007.06.140; PII: S0006-291X(07)01420-9; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
Similar Records
Locations of the three primary binding sites for long-chain fatty acids on bovine serum albumin
STUDIES ON THE GAMMA RAY IRRADIATION ON THE PROTEIN. II. THE ESR ABSORPTION OF PROTEINS, AMINO ACIDS, AND PEPTIDES