C-Terminal Identification of AD74, a Proteolytic Product of Enterococcus faecalis Aggregation Substance: Application of Liquid Chromatography/Mass Spectrometry

Jiro Nakayama, Hiroshi Watarai, Akira Isogai, Akinori Suzuki

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3 Citations (Scopus)


Sexual aggregation involved in conjugative transfer of Enterococcus faecalis plasmid pADl is enhanced by the sex pheromone cADl, which is excreted from recipient cells. A membrane-anchored 137 kDa protein is a pADl-encoded aggregation substance designated asal, which is responsible for cell-cell contact and leads to the aggregation of cells. An AD74 protein is a proteolytic product corresponding to the N-terminal half of asal. The C-terminal of AD74 was identified as lysine at position 510 (K-510) by liquid chromatography/mass spectrometry (LC/MS): it indicates that asal is cleaved specifically between K-510 and G-511.

Original languageEnglish
Pages (from-to)127-131
Number of pages5
JournalBioscience, biotechnology, and biochemistry
Issue number1
Publication statusPublished - Jan 1 1992
Externally publishedYes


All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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