FORMATION AND PROPERTIES OF OXOACYL FLUORESCENT DERIVATIVE ON N-TERMINALS OF PROTEINS AND PEPTIDES
肽链及蛋白质N-末端羰酰荧光衍生物的形成

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.