TRYPTIC PEPTIDE-MAPPING OF SEQUENCE 1-298 OF HUMAN SERUM-ALBUMIN BY HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY AND FAST-ATOM-BOMBARDMENT MASS-SPECTROMETRY

The determination of the tryptic peptide mapping of sequence 1-298 of human serum albumin (HSA) by chemical and enzymatic cleavage and combi ned use of high-performance liquid chromatography (HPLC) and fast-atom bombardment mass spectrometry (FAB-MS) is described. A total coverage of about 75% of the entire sequence was obtained. Unidentified fragme nts included some peptides which were not present in the chromatograms because of their extreme hydrophobic or hydrophilic character, as ind icated by the calculated retention times. Due to the high reproducibil ity of the experiments and to the satisfactory yield of the tryptic fr agments identified, the combined use of HPLC and FAB-MS appears to pos sess great potential for structural investigation of HSA.