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

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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
Volume56
Issue number1
DOIs
Publication statusPublished - Jan 1 1992
Externally publishedYes

Fingerprint

Liquid chromatography
Liquid Chromatography
Mass spectrometry
Mass Spectrometry
Agglomeration
Sex Attractants
Cell Aggregation
Enterococcus faecalis
Lysine
Proteins
Plasmids
Membranes
Enterococcus faecalis aggregation substance

All Science Journal Classification (ASJC) codes

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

Cite this

C-Terminal Identification of AD74, a Proteolytic Product of Enterococcus faecalis Aggregation Substance : Application of Liquid Chromatography/Mass Spectrometry. / Nakayama, Jiro; Watarai, Hiroshi; Isogai, Akira; Suzuki, Akinori.

In: Bioscience, Biotechnology, and Biochemistry, Vol. 56, No. 1, 01.01.1992, p. 127-131.

Research output: Contribution to journalArticle

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