Spectroscopic studies of the interaction of anti-coagulant rodenticide diphacinone with human serum albumin

Milk β-lactoglobulin complexes with tea polyphenols

“…The fluorescence spectra were recorded at k exc = 280 nm and k emi from 290 to 500 nm. The intensity at 340 nm (tryptophan) was used to calculate the binding constant (K) according to previous literature reports (Bi et al, 2004;Dufour & Dangles, 2005;He et al, 2005;Tang, Qi, & Chen, 2005).…”

Interaction of milk α- and β-caseins with tea polyphenols

“…The fluorescence spectra were recorded at k exc = 280 nm and k em from 287 to 500 nm. The intensity at 350 nm (tryptophan) was used to calculate the binding constant (K) according to previous literature reports (Bi et al, 2004;Dufour & Dangles, 2005;He et al, 2005;Tang, Qi, & Chen, 2005).…”

Folic acid complexes with human and bovine serum albumins

“…The fluorescence spectra were recorded at k exc = 280 nm and k em from 287 to 500 nm. The intensity at 347 nm (tryptophan) was used to calculate the binding constant (K) according to previous literature reports (Bi et al, 2004;Dufour & Dangles, 2005;He et al, 2005;Tang, Qi, & Chen, 2005).…”