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- W2384007609 abstract "The interaction between 4-nitroaniline and bovine serum albumin(BSA) was investigated by fluorescence under the imitated physiological condition of animal body.4-Nitroaniline can strongly quench intrinsic fluorescence of BSA.In the mechanism discussion,it is proved that static quenching occurs predominately.According to Stern-Volmer equation and double-log regression equation,we found that BSA reacted with 4-nitroanline and formed a certain new compound.The binding constants K(298 K:2.18×104 L/mol;310 K:1.95×104 L/mol) and the number of binding site n(298K∶1.09;310 K∶1.12)were obtained using double-log regression equation.Negative enthalpy(ΔH) and positive entropy(ΔS) values indicated that both hydrogen bond and hydrophobic forces played a major role in the binding of 4-nitroaniline and BSA.The results of synchronous fluorescence show that the conformation of BSA has changed in the presence of 4-nitroaniline and the hydrophobicity around tryptophanyl and tyrosyl residues increased." @default.
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- W2384007609 date "2011-01-01" @default.
- W2384007609 modified "2023-09-25" @default.
- W2384007609 title "Interaction of 4-nitoraniline with bovine serum albumin by fluorescence spectroscopy" @default.
- W2384007609 hasPublicationYear "2011" @default.
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