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- W2379805495 abstract "Objective To study the interaction between bovine serum albumin(BSA) and rhein or its complexes. Methods Spectroscopic methods were utilized to determine the binding data.Stern-Volmer equation was used to process the data. Results Rhein and its complexes could significantly quench the endogenous fluorescence of BSA mainly by a static mode.The binding constants Kb of RH-Fe,RH-Co and RH-Mn with BSA are 3.55×105 L/mol,2.46×105 L/mol,4.83×105 L/mol,1.87×105 L/mol,3.55×105 L/mol and 2.46×105L/mol at 293K and 300K,respectively.From the thermodynamics parameter judge,we can learn that the major forces between rhein or its complexes and the BSA are vander walls force and hydrogen bond.Based on Frster non-radiation energy transfer mechanism,the binding site were found to be an area of 2.22,2.57.3.14 and 2.59 nm away from tryptophan residue in BSA for RH,RH-Co,RH-Fe and RH-Mn,respectively.The results also show that the binding constant of RH with BSA can be affected by coexistence of Co2+,Mn2+,Fe2+ in the same temperatun. Conclusion The binding ability of RH with BSA can significantly enhance after forming metal complexes and then affect the storage and transportation of RH and metal ions." @default.
- W2379805495 created "2016-06-24" @default.
- W2379805495 creator A5066272361 @default.
- W2379805495 date "2013-01-01" @default.
- W2379805495 modified "2023-09-23" @default.
- W2379805495 title "Interaction of Bovine Serum Albumin with Rhein and its Metal Complexes" @default.
- W2379805495 hasPublicationYear "2013" @default.
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