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) | 85-89 |
| Number of pages | 5 |
| Journal | FEMS Microbiology Letters |
| Volume | 77 |
| Issue number | 1 |
| Publication status | Published - Jan 1 1991 |
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Keywords
- Actinobacillus actinomycetemcomitans
- Major outer membrane protein (MOMP)
ASJC Scopus subject areas
- Genetics
- Molecular Biology
- Applied Microbiology and Biotechnology
- Microbiology
Cite this
Isolation and partial characterization of a 39 kDa major outer membrane protein of Actinobacillus actinomycetemcomitans Y4. / Kokeguchi, Susumu; Kato, Keijiro; Nishimura, Fusanori; Kurihara, Hidemi; Murayama, Yoji.
In: FEMS Microbiology Letters, Vol. 77, No. 1, 01.01.1991, p. 85-89.Research output: Contribution to journal › Article
}
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.
KW - Actinobacillus actinomycetemcomitans
KW - Major outer membrane protein (MOMP)
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UR - http://www.scopus.com/inward/citedby.url?scp=0025982587&partnerID=8YFLogxK
M3 - Article
C2 - 2004699
AN - SCOPUS:0025982587
VL - 77
SP - 85
EP - 89
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
SN - 0378-1097
IS - 1
ER -