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

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10.1271/bbb.56.127

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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, 1992, p. 127-131.

Research output: Contribution to journal › Article › peer-review

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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. Copyright: Copyright 2016 Elsevier B.V., All rights reserved.",

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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. Copyright: Copyright 2016 Elsevier B.V., All rights reserved.

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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.

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

Abstract

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