Isolation and partial characterization of a 39 kDa major outer membrane protein of Actinobacillus actinomycetemcomitans Y4.
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.
Kokeguchi
S
S
Department of Oral Microbiology, Okayama University Dental School, Japan.
Kato
K
K
Nishimura
F
F
Kurihara
H
H
Murayama
Y
Y
D000188:Actinobacillus / Q000032:analysis* / Q000187:drug effects; D000595:Amino Acid Sequence; D000906:Antibodies / Q000276:immunology; D001425:Bacterial Outer Membrane Proteins / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003902:Detergents / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010518:Periodontitis / Q000276:immunology; D012689:Sequence Homology, Nucleic Acid
D000906:Antibodies; D001425:Bacterial Outer Membrane Proteins; D003902:Detergents