pH-induced conformational transitions of bovine serum albumin investigated by ultraviolet derivative spectroscopy

doi:10.7523/j.issn.2095-6134.2011.1.003

Abstract

Abstract:

The fine absorption bands of three aromatic amino acid residues,Tryptophan (Trp),Tyrosine (Tyr),and Phenylalanine (Phe),of bovine serum albumin (BSA) were studied by ultraviolet second derivative spectroscopy.The conformation transitions of BSA at pH 2.3-12 were analyzed along with the absorption spectrum of the peptide bonds.It is observed that there exist obvious conformation transitions around the isoelectric point (pH 4.7) of BSA.The transitions are subtle between pH 5.7 and pH 10 but distinct in strong acidity(pH 2.3) and alkaline(pH 12) environments. Meanwhile,the concentration of BSA has certain effect on the conformation transition.

Key words: bovine serum albumin(BSA), conformational transition, ultraviolet derivative spectroscopy

CLC Number:

Q512.1

PENG Gang, LIU Bai-Ling, ZHAO Chun-Xia, JIANG Zheng-Wu. pH-induced conformational transitions of bovine serum albumin investigated by ultraviolet derivative spectroscopy[J]. , 2011, 28(1): 12-18.

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