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.
ASJC Scopus subject areas
- Molecular Medicine