收稿日期: 2010-03-31
修回日期: 2010-05-17
网络出版日期: 2011-01-20
基金资助
国家自然科学基金(20974111)资助
pH-induced conformational transitions of bovine serum albumin investigated by ultraviolet derivative spectroscopy
Received date: 2010-03-31
Revised date: 2010-05-17
Online published: 2011-01-20
彭钢 , 刘白玲 , 赵春霞 , 江正武 . 导数紫外光谱法研究pH诱导牛血清蛋白构象变化[J]. 中国科学院大学学报, 2011 , 28(1) : 12 -18 . DOI: 10.7523/j.issn.2095-6134.2011.1.003
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.
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