ISOLATION AND PARTIAL CHARACTERIZATION OF A 39 KDA MAJOR OUTER-MEMBRANE PROTEIN OF ACTINOBACILLUS-ACTINOMYCETEMCOMITANS Y4

被引：14
|
作者：
KOKEGUCHI, S
KATO, K
NISHIMURA, F
KURIHARA, H
MURAYAMA, Y
机构：
[1] OKAYAMA UNIV,SCH DENT,DEPT ORAL MICROBIOL,5-1 SHIKATA CHO,2-CHOME,OKAYAMA 700,JAPAN
[2] OKAYAMA UNIV,SCH DENT,DEPT PERIODONTOL & ENDODONTOL,OKAYAMA 700,JAPAN
来源：
FEMS MICROBIOLOGY LETTERS | 1991年 / 77卷 / 01期
关键词：
ACTINOBACILLUS ACTINOMYCETEMCOMITANS; MAJOR OUTER MEMBRANE PROTEIN (MOMP);
D O I：
10.1016/0378-1097(91)90018-6
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
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 kDa MOMP of A. actinomycetemcomitans were 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.
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页码：85 / 89
页数：5
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