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- W2384007192 abstract "The interaction mechanism and thermodynamic characteristic between reduced nicotinamide adenine dinucleotide(NADH)and human serum albumin(HSA)have been investigated by fluorescence spectrometry,UV spectroscopy and molecular modeling.The fluorescence quenching of HSA by NADH indicates that the mechanism is a static quenching.The bonding constants and the binding point numbers of NADH and HSA are KA1=1.972×104L.mol-1,n1=0.9657(283K)and KA2=1.468×104 L.mol-1,n2=0.9105(310K),respectively.The thermodynamic parameters were calculated according to the Van’t Hoff equation.Synchronous spectra shows that the microenvironment of tryptophan residues is more hydrophilic when NADH is added.Molecular modeling suggests that NADH is located in subdomainⅡA into HSA by hydrophobic forces,electrostatic and hydrogen bond." @default.
- W2384007192 created "2016-06-24" @default.
- W2384007192 creator A5043123697 @default.
- W2384007192 date "2013-01-01" @default.
- W2384007192 modified "2023-09-28" @default.
- W2384007192 title "Study on the Interaction of Reduced Nicotinamide Adenine Dinucleotide with Human Serum Albumin" @default.
- W2384007192 hasPublicationYear "2013" @default.
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