%0 Journal Article
%T FORMATION AND PROPERTIES OF OXOACYL FLUORESCENT DERIVATIVE ON N-TERMINALS OF PROTEINS AND PEPTIDES<br>肽链及蛋白质N-末端羰酰荧光衍生物的形成
%A He Rongqiao
%A Tsou Chenlu
%A <br>赫荣乔
%A 邹承鲁
%J 生物物理学报
%D 1991
%I 
%X Dixon transamination of oligopeptides and insulin results in the formation of a fluorescent derivative having emission maximum about 398-408nm with 0.02-0.03 quantum yield by the excitation at 3l2-333nm depending on the nature and length of the peptide. The chemical structure of the fluorophore may be ?-Oxo-acyl-amide which would be effected by thd second and the third amino acid residues, its intensity decreases when pH>9.0 and increases with the increment of concentrations of NaCl solution. Changes of the Oxoacyl-amide fluorescence of oligopeptides are comparatively different with their different kinds or configurations of the composed residues. It is suggested that such a fluorescence derivative may be used as a probe for the study of the conformation of the N-terminal region of peptides and proteins.
%K N-terminal
%K Fluorescent derivative
%K Dixon transamination<br>肽链
%K 蛋白
%K 末端
%K 荧光衍生物
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=5E86E445AE6962DC41744C09239A74C4&yid=116CB34717B0B183&vid=DF92D298D3FF1E6E&iid=E158A972A605785F&sid=389DA78D878702A9&eid=8D75AD3BD0D1BCC5&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=1&reference_num=5