β Scribed by Ernesto Estrada; Eugenio Uriarte; Enrique Molina; Yamil Simon-Manso; George W. A. Milne
No coin nor oath required. For personal study only.
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Binding of ibuprofen (IB) enantiomers to human serum albumin (HSA) was studied using a chiral fluorescent derivatizing reagent, which enabled the measurement of IB enantiomers at a concentration as low 5 x 10(-8) M. Scatchard analyses revealed that there were two classes of binding sites for both en
A technique based on a human serum albumin (HSA) stationary phase high-pressure liquid chromatography (HPLC) has been successfully used for the past few years to characterize the interactions between HSA and new substrates. Immobilized HSA conserves the binding properties of the protein in solution,
The binding of racemic, (R)([) and (S)(])-ibuprofen (IBP) to human serum albumin (HSA) was studied using NMR spectroscopy. Having saturated the tight binding sites, the extent of weak binding was then investigated. The molecular di β usion coefficients of IBP in HSA solution at di β erent concentratio
The stereoselectivity of the reversible binding interactions between the Dand L-tryptophan enantiomers and serum albumins of different animal species and fragments of human serum albumin (HSA) was investigated by applying three novel high performance liquid chromatographic (HPLC) arrangements. The s