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- W2382256898 abstract "The interaction between two anthraquinones(rhein and emodin) and model protein(bovine serum albumin) was investigated by fluorescence quenching technique and infrared spectroscopy.The results showed that rhein and emodin mainly formed ground-state complex with bovine serum albumin by electrostatic interaction,which led to the quenching of intrinsic fluorescence of bovine serum albumin.The binding constant,number of binding site and the distance between rhein,emodin and tryptophan residue were determined.Some metal ions had effect on the binding of these two anthraquinones and bovine serum albumin.The infrared spectra showed that both rhein and emodin induced secondary structure change of bovine serum albumin.The interaction was also compared with other three anthraquinones,which indicated that the number of phenolic hydroxyl group and the polarity of the substituent group on C(3) had a significant effect on the activity of the compounds." @default.
- W2382256898 created "2016-06-24" @default.
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- W2382256898 date "2011-01-01" @default.
- W2382256898 modified "2023-09-25" @default.
- W2382256898 title "Interaction of Rhein and Emodin with Bovine Serum Albumin" @default.
- W2382256898 hasPublicationYear "2011" @default.
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