Fragmentation of proteins in the 13- to 29-kDa mass range observed by 252Cf-plasma desorption mass spectrometry.
Results are presented on the observation of sequence-specific fragmentation of proteins in the 13- to 29-kDa mass range (ribonuclease A, papain, and proteinase K) by 252Cf-plasma desorption mass spectrometry. For these proteins, extensive N-terminal an, cn + 2, and dn fragment ions are observed with mass accuracies approaching 200 ppm for the most prominent fragment ions. The fragmentation pattern of these proteins shows the same fundamental behavior (arginine-directed, charge-remote fragmentation) that is observed in the fragmentation of small peptides, indicating that similar processes are occurring when large proteins and small peptides fragment in plasma desorption mass spectrometry.
Bunk
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DM
Department of Chemistry, Texas A&M University, College Station 77843-3255.
Macfarlane
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RD
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D019286:Endopeptidase K; D066298:In Vitro Techniques; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010206:Papain / Q000737:chemistry*; D010446:Peptide Fragments / Q000032:analysis*; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*; D012697:Serine Endopeptidases / Q000737:chemistry*
D010446:Peptide Fragments; D012259:Ribonuclease, Pancreatic; D012697:Serine Endopeptidases; D019286:Endopeptidase K; D010206:Papain