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.
The capacity of human serum albumin to bind bilirubin is of paramount importance in the prevention of neurological damage due to hyperbilirubinemia in the neonate. Currently, there is no rapid, reliable method to determine the reserve bilirubin loading capacity of serum albumin. A method using electron spin resonance spectroscopy with a dianionic
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