Preparative capillary electrophoresis and mass spectrometry for the identification of a putative heparin-binding site in amyloid P component.
A heparin-binding peptide fragment from chymotrypsin-treated human serum amyloid P component (SAP) was demonstrated by affinity CE. The peptide was found in a fraction of peptides that were not separated well by reversed-phase HPLC. On the basis of mass determination by laser desorption mass spectrometry after preparative CE, the fragment could be placed in the parent protein structure. Thus, in the course of the study of structure-function relationships of SAP, CE was helpful for the examination of peptide fragments from proteolytic digests that were poorly separated by standard reversed-phase HPLC methods and for the purification of peptides in the mixture.
Heegaard
N H
NH
Department of Autoimmunology, Statens Seruminstitut, Copenhagen S, Denmark.
Roepstorff
P
P
D001665:Binding Sites; D019075:Electrophoresis, Capillary; D006493:Heparin / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D013058:Mass Spectrometry; D000683:Serum Amyloid P-Component / Q000737:chemistry* / Q000378:metabolism
D000683:Serum Amyloid P-Component; D006493:Heparin