The binding isotherms for the interaction of 5-doxyl stearic acid with bovine and human albumin.
作者： S J Rehfeld , D J Eatough , W Z Plachy
DOI: 10.1016/S0022-2275(20)40697-2
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摘要: Binding isotherms for the interaction of 5-doxyl stearic acid with bovine and human albumin are reported. The critical micelle concentration (CMC) limiting solubility were determined using electron spin resonance (ESR)-spin label method. CMC this spin-label in saline-phosphate buffer 3.5 x 10(-5) M 2 10(-4) M, respectively. We found no ESR line width evidence pre-association stearate below CMC. Maximum binding to both occurs before formation. isotherm is agreement data obtained by others [1-(14)C]stearic acid. For albumin, comparison difficult since previous vary widely. Comparison 2T(||) values (the splitting between low high field extremes, a measure degree immobilization protein-bound stearate) indicates greater molecules bound albumin. indicate that complexes formed stearate/albumin ratios at least 18. computed equilibrium constants first seven tightly bound, log K > 5.0. species predicted form solution these
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