Open AccessIsolation and partial characterization of a 39 kDa major outer membrane protein of Actinobacillus actinomycetemcomitans Y4
Author(s) -
Kokeguchi Susumu,
Kato Keijiro,
Nishimura Fusanori,
Kurihara Hidemi,
Murayama Yoji
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb04326.x
Subject(s) - bacterial outer membrane , actinobacillus , size exclusion chromatography , ion chromatography , peptide sequence , biochemistry , cyanogen bromide , amino acid , chemistry , chromatography , bacteria , molecular mass , biology , microbiology and biotechnology , escherichia coli , enzyme , gene , genetics
Summary The outer membrane fractions of Actinobacillus actinomycetemcomitans , which were extracted from whole cells with cetyl trimethyl ammonium bromide and CaCl 2 , 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.