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

doi:10.1271/bbb.56.127

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 journal › Article › peer-review

5 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 language	English
Pages (from-to)	127-131
Number of pages	5
Journal	Bioscience, biotechnology, and biochemistry
Volume	56
Issue number	1
DOIs	https://doi.org/10.1271/bbb.56.127
Publication status	Published - 1992
Externally published	Yes

All Science Journal Classification (ASJC) codes

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

Access to Document

10.1271/bbb.56.127

Cite this

@article{b1e004d452334d83bdfadea60ec619c7,

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

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.",

author = "Jiro Nakayama and Hiroshi Watarai and Akira Isogai and Akinori Suzuki",

note = "Funding Information: Acknowledgment. This work was partly supported by a Grant-in~Aid for Scientific Research from the Ministry of Education, Science, and Culture of Japan.",

year = "1992",

doi = "10.1271/bbb.56.127",

language = "English",

volume = "56",

pages = "127--131",

journal = "Bioscience, Biotechnology and Biochemistry",

issn = "0916-8451",

publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",

number = "1",

}

TY - JOUR

T1 - C-Terminal Identification of AD74, a Proteolytic Product of Enterococcus faecalis Aggregation Substance

T2 - Application of Liquid Chromatography/Mass Spectrometry

AU - Nakayama, Jiro

AU - Watarai, Hiroshi

AU - Isogai, Akira

AU - Suzuki, Akinori

N1 - Funding Information: Acknowledgment. This work was partly supported by a Grant-in~Aid for Scientific Research from the Ministry of Education, Science, and Culture of Japan.

PY - 1992

Y1 - 1992

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0026485964&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026485964&partnerID=8YFLogxK

U2 - 10.1271/bbb.56.127

DO - 10.1271/bbb.56.127

M3 - Article

C2 - 1368124

AN - SCOPUS:0026485964

VL - 56

SP - 127

EP - 131

JO - Bioscience, Biotechnology and Biochemistry

JF - Bioscience, Biotechnology and Biochemistry

SN - 0916-8451

IS - 1

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this