Peptide profiles of surface-labeled proteins shed or released by enzyme digestion from staphylococcus aureus determined by reverse phase high performance liquid chromatography

B. A. Sanford, V. L. Thomas, M. A. Ramsay, T. O. Jones

Research output: Contribution to journalArticlepeer-review

Abstract

The surface proteins of Staphylococcus aureus were radiolabeled and subsequently characterized by autoradiography and reverse phase-high performance liquid chromatography. Approximately 25% of the surface-labeled proteins were shed from non-growing cells; the shed proteins contributed to the labeled-protein pool obtained by protease digestion of whole cells. The elution profiles of I-labeled peptides allowed direct comparisons of shed surface proteins (untreated or protease digested) with surface proteins cleaved from the cells by protease treatment.

Original languageEnglish (US)
Pages (from-to)1577-1589
Number of pages13
JournalJournal of Liquid Chromatography
Volume9
Issue number7
DOIs
StatePublished - May 1 1986

ASJC Scopus subject areas

  • Molecular Medicine

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