Abstract:
: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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Gurachevsky A,Shimanovitch E,Gurachevskaya T,Muravsky Vdoi
10.1016/j.bbrc.2007.06.140subject
Has Abstractpub_date
2007-09-07 00:00:00pages
852-6issue
4eissn
0006-291Xissn
1090-2104pii
S0006-291X(07)01420-9journal_volume
360pub_type
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