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

13 Citations (Scopus)

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
Externally published	Yes

All Science Journal Classification (ASJC) codes

Microbiology
Molecular Biology
Genetics

Access to Document

10.1111/j.1574-6968.1991.tb04326.x

Cite this

@article{1393bc935ebf48e2ac21908926d99784,

title = "Isolation and partial characterization of a 39 kDa major outer membrane protein of Actinobacillus actinomycetemcomitans Y4",

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.",

author = "Susumu Kokeguchi and Keijiro Kato and Fusanori Nishimura and Hidemi Kurihara and Yoji Murayama",

year = "1991",

month = jan,

day = "1",

doi = "10.1111/j.1574-6968.1991.tb04326.x",

language = "English",

volume = "77",

pages = "85--90",

journal = "FEMS microbiology letters",

issn = "0378-1097",

publisher = "Wiley-Blackwell",

number = "1",

}

TY - JOUR

T1 - Isolation and partial characterization of a 39 kDa major outer membrane protein of Actinobacillus actinomycetemcomitans Y4

AU - Kokeguchi, Susumu

AU - Kato, Keijiro

AU - Nishimura, Fusanori

AU - Kurihara, Hidemi

AU - Murayama, Yoji

PY - 1991/1/1

Y1 - 1991/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0025982587&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025982587&partnerID=8YFLogxK

U2 - 10.1111/j.1574-6968.1991.tb04326.x

DO - 10.1111/j.1574-6968.1991.tb04326.x

M3 - Article

C2 - 2004699

AN - SCOPUS:0025982587

SN - 0378-1097

VL - 77

SP - 85

EP - 90

JO - FEMS microbiology letters

JF - FEMS microbiology letters

IS - 1

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this