Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1992 Jul 1;89(13):6215–6219. doi: 10.1073/pnas.89.13.6215

Fragmentation of proteins in the 13- to 29-kDa mass range observed by 252Cf-plasma desorption mass spectrometry.

D M Bunk 1, R D Macfarlane 1
PMCID: PMC402153  PMID: 1631112

Abstract

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.

Full text

PDF
6215

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Biemann K. Contributions of mass spectrometry to peptide and protein structure. Biomed Environ Mass Spectrom. 1988 Oct;16(1-12):99–111. doi: 10.1002/bms.1200160119. [DOI] [PubMed] [Google Scholar]
  2. Cohen L. W., Coghlan V. M., Dihel L. C. Cloning and sequencing of papain-encoding cDNA. Gene. 1986;48(2-3):219–227. doi: 10.1016/0378-1119(86)90080-6. [DOI] [PubMed] [Google Scholar]
  3. Fordham-Skelton A. P., Yarwood A., Croy R. R. Synthesis of saporin gene probes from partial protein sequence data: use of inosine-oligonucleotides, genomic DNA and the polymerase chain reaction. Mol Gen Genet. 1990 Mar;221(1):134–138. doi: 10.1007/BF00280379. [DOI] [PubMed] [Google Scholar]
  4. Loo J. A., Edmonds C. G., Smith R. D. Primary sequence information from intact proteins by electrospray ionization tandem mass spectrometry. Science. 1990 Apr 13;248(4952):201–204. doi: 10.1126/science.2326633. [DOI] [PubMed] [Google Scholar]
  5. Pähler A., Banerjee A., Dattagupta J. K., Fujiwara T., Lindner K., Pal G. P., Suck D., Weber G., Saenger W. Three-dimensional structure of fungal proteinase K reveals similarity to bacterial subtilisin. EMBO J. 1984 Jun;3(6):1311–1314. doi: 10.1002/j.1460-2075.1984.tb01968.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Roepstorff P., Fohlman J. Proposal for a common nomenclature for sequence ions in mass spectra of peptides. Biomed Mass Spectrom. 1984 Nov;11(11):601–601. doi: 10.1002/bms.1200111109. [DOI] [PubMed] [Google Scholar]
  7. Wlodawer A., Bott R., Sjölin L. The refined crystal structure of ribonuclease A at 2.0 A resolution. J Biol Chem. 1982 Feb 10;257(3):1325–1332. [PubMed] [Google Scholar]
  8. Wlodawer A., Sjölin L. Structure of ribonuclease A: results of joint neutron and X-ray refinement at 2.0-A resolution. Biochemistry. 1983 May 24;22(11):2720–2728. doi: 10.1021/bi00280a021. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES