ANALYSIS OF PEPTIDES FROM BOVINE HEMOGLOBIN AND TUNA MYOGLOBIN ENZYMATIC HYDROLYSATE - USE OF HPLC WITH ONLINE 2ND-ORDER DERIVATIVE SPECTROSCOPY FOR THE CHARACTERIZATION OF BIOLOGICALLY-ACTIVE PEPTIDES

The chromatographic resolution of bovine hemoglobin and tuna myoglobin peptic hydrolysates was performed by use of successive SE- and RP-HPL C in order to obtain pure peptides. Analysis of their amino acid compo sition and second order derivative spectroscopy allowed us to determin e the accurate identity of these peptides and consequently to locate t hem in both protein sequences. Some biologically activity peptides gen erated from hemoglobin were also studied by these methods to investiga te the kinetics of their appearance during peptic hydrolysis. (C) 1997 Elsevier Science B.V.