%0 Journal Article
%T pH-induced conformational transitions of bovine serum albumin investigated by ultraviolet derivative spectroscopy<br>导数紫外光谱法研究pH诱导牛血清蛋白构象变化
%A PENG Gang
%A LIU Bai-Ling
%A ZHAO Chun-Xia
%A JIANG Zheng-Wu
%A <br>彭钢
%A 刘白玲
%A 赵春霞
%A 江正武
%J 中国科学院研究生院学报
%D 2011
%I 
%X 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.
%K bovine serum albumin(BSA)
%K conformational transition
%K ultraviolet derivative spectroscopy<br>牛血清蛋白
%K 构象变化
%K 导数紫外光谱
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=B5EDD921F3D863E289B22F36E70174A7007B5F5E43D63598017D41BB67247657&cid=B47B31F6349F979B&jid=67CDFDECD959936E166E0F72DE972847&aid=8F987AC0E9D37468493CD38E17F8FBE7&yid=9377ED8094509821&vid=D3E34374A0D77D7F&iid=CA4FD0336C81A37A&sid=59906B3B2830C2C5&eid=13553B2D12F347E8&journal_id=1002-1175&journal_name=中国科学院研究生院学报&referenced_num=0&reference_num=14