Degradation of penicillin-binding protein 2' in methicillin-resistant staphylococcus aureus

Y. Sumita, M. Fukasawa, S. Mitsuhashi, M. Inoue

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


We detected a novel protein with [14C]benzylpenicillin (PCG)- binding capacity and a molecular mass of about 60 kD in meth- icillin-resistant Staphylococcus aureus using a high concentration of [14C]PCG and extending the reaction time. However, the fluorogram showed that the band density of penicillin- binding protein 2' (PBP2') decreased gradually with incubation time. The appearance of the 60-kD protein and the reduction of the band density of PBP2' were stoichiometrically linked, and the binding profiles of p-lactams for PBP2' and the 60-kD protein corresponded. These results suggested that the 60-kD protein is a degradation product of PBP2.

Original languageEnglish
Pages (from-to)172-177
Number of pages6
Issue number3
Publication statusPublished - Jan 1 1995


  • Degradation
  • Mcthicillin-resistant
  • P-Lactams
  • Penicillin-binding protein 2
  • Staphylococcus aureus

ASJC Scopus subject areas

  • Oncology
  • Pharmacology
  • Drug Discovery
  • Pharmacology (medical)
  • Infectious Diseases


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