Bovine serum albumin: characterization of a fatty acid binding site on the N-terminal peptic fragment using a new spin-label

A new spin-label, 4-(L-glutamo)-4'-[(1-oxy-2,2,5,5-tetramethyl-3L-pyrrolidinyl )amino]-3, 3'-dinitrodiphenyl sulfone, is shown to bind to one high-affinity binding site on bovine serum albumin (K = 5 X 10(4) M-1, n = 1). Analysis of the binding of the spin-label to the amino-terminal half...

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Bibliographic Details
Published in:Biochemistry (Easton) 1984-12, Vol.23 (25), p.5930-5932
Main Authors: Hsia, J. C, Wong, L. T, Tan, C. T, Er, S. S, Kharouba, S, Balaskas, E, Tinker, D. O, Feldhoff, R. C
Format: Article
Language:English
Subjects:
Binding Sites
Biological and medical sciences
Electron Spin Resonance Spectroscopy
Fatty Acids - metabolism
Fundamental and applied biological sciences. Psychology
Glutamine - analogs & derivatives
Glutamine - metabolism
Interactions. Associations
Intermolecular phenomena
Molecular biophysics
Palmitates - metabolism
Peptide Fragments - metabolism
Serum Albumin, Bovine - metabolism
Spin Labels
Sulfones - metabolism
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Summary:A new spin-label, 4-(L-glutamo)-4'-[(1-oxy-2,2,5,5-tetramethyl-3L-pyrrolidinyl )amino]-3, 3'-dinitrodiphenyl sulfone, is shown to bind to one high-affinity binding site on bovine serum albumin (K = 5 X 10(4) M-1, n = 1). Analysis of the binding of the spin-label to the amino-terminal half (peptic fragment PB) and the carboxy-terminal half (peptic fragment PA) of BSA, and their complex (PA-PB), indicates that the spin-label binds to a long-chain fatty acid binding site located on PB. The usefulness of the novel specificity of the spin-label in characterizing this binding site is discussed.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00320a006