Biochemical properties of the major outer membrane proteins of Porphyromonas gingivalis.
The major outer membrane proteins (MOMP) of 53 and 67 kDa were identified by sodium dodecyl sulphate-polyacrylamide gel electrophoresis in outer membrane enriched fractions of Porphyromonas gingivalis FDC 381 and ATCC 33277, respectively. The MOMP were purified by anion exchange and gel filtration chromatography after extraction with Zwittergent 3-14. Their reactivity to monoclonal antibodies and their amino acid composition were analysed. The N-terminal amino acid sequences of twenty residues of both purified MOMP were determined and compared with those previously reported for MOMP of other periodontopathic bacteria.
Kokeguchi
S
S
Department of Oral Microbiology, Okayama University Dental School, Japan.
Miyamoto
M
M
Ohyama
H
H
Hongyo
H
H
Takigawa
M
M
Kurihara
H
H
Murayama
Y
Y
Kato
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification; D006801:Humans; D007106:Immune Sera; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010518:Periodontitis / Q000276:immunology; D016966:Porphyromonas gingivalis / Q000737:chemistry*; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
D000596:Amino Acids; D000911:Antibodies, Monoclonal; D001425:Bacterial Outer Membrane Proteins; D007106:Immune Sera