Isolation and partial characterization of a 39 kDa major outer membrane protein of Actinobacillus actinomycetemcomitans Y4

Susumu Kokeguchi; Keijiro Kato; Fusanori Nishimura; Hidemi Kurihara; Yoji Murayama

doi:10.1111/j.1574-6968.1991.tb04326.x

Isolation and partial characterization of a 39 kDa major outer membrane protein of Actinobacillus actinomycetemcomitans Y4

Susumu Kokeguchi, Keijiro Kato, Fusanori Nishimura, Hidemi Kurihara, Yoji Murayama

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

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Abstract

The outer membrane fractions of Actinobacillus actinomycetemcomitans, which were extracted from whole cells with cetyl trimethyl ammonium bromide and CaCl₂, contained four major outer membrane proteins (MOMP) of 39, 37, 36 and 30 kDa. The 39 kDa MOMP of A. actinomycetemcomitans was sequentially purified by extraction with Zwittergent 3-14 detergent, anion-exchange chromatography and gel filtration chromatography. Analysis of amino acid composition and N-terminal amino acid sequence of 20 residues of purified 39 kDa MOMP was performed. Although some of the periodontitis patient sera reacted strongly with 39 kDa and 30 kDa MOMP in crude outer membrane fractions, purified 39 kDa MOMP showed decreased immunoreactivity with the human sera.

Original language	English
Pages (from-to)	85-90
Number of pages	6
Journal	FEMS Microbiology Letters
Volume	77
Issue number	1
DOIs	https://doi.org/10.1111/j.1574-6968.1991.tb04326.x
Publication status	Published - Jan 1 1991

Keywords

Actinobacillus actinomycetemcomitans
Major outer membrane protein (MOMP)

ASJC Scopus subject areas

Microbiology
Molecular Biology
Genetics

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abstract = "The outer membrane fractions of Actinobacillus actinomycetemcomitans, which were extracted from whole cells with cetyl trimethyl ammonium bromide and CaCl2, contained four major outer membrane proteins (MOMP) of 39, 37, 36 and 30 kDa. The 39 kDa MOMP of A. actinomycetemcomitans was sequentially purified by extraction with Zwittergent 3-14 detergent, anion-exchange chromatography and gel filtration chromatography. Analysis of amino acid composition and N-terminal amino acid sequence of 20 residues of purified 39 kDa MOMP was performed. Although some of the periodontitis patient sera reacted strongly with 39 kDa and 30 kDa MOMP in crude outer membrane fractions, purified 39 kDa MOMP showed decreased immunoreactivity with the human sera.",

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AU - Kato, Keijiro

AU - Nishimura, Fusanori

AU - Kurihara, Hidemi

AU - Murayama, Yoji

PY - 1991/1/1

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Isolation and partial characterization of a 39 kDa major outer membrane protein of Actinobacillus actinomycetemcomitans Y4

Abstract

Keywords

ASJC Scopus subject areas

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