%0 Journal Article
%T PURIFICATION AND CHARACTERIZATION OF S-LAYER PROTEIN FROM AEROMONAS HYDROPHILA<br>嗜水气单胞菌S蛋白的提纯及特性分析
%A Yan Yaxian Chen Huaiqing Lu Chengping
%A <br>严亚贤
%A 陈怀青
%A 陆承平
%J 微生物学报
%D 1996
%I 
%X The regular surface protein array (S-layer) present on Aeromonas hydrophila J-l was composed of a single species of protein of apparent molecular weight 51500. This protein was extracted from whole cells by treatment with 0.2mol / L glycine hydrocholoide (pH4.0). The protein was purified by Sephadex G-200 gel filtration chromatography and an ion exchange chromatography on DEAE-cellulose. Amino acid composition analysis showed, that the protein contained 36.8% hydrophobic amino acids. But the protein did not confer hydrophobicity to the cell surface when present as an intact S-layer by salt aggregation test. ELISA and immunoblotting with two different polyclonal antisera against surface exposed-(PM)and non-surface-exposed epitopes (PR) of the protein revealed that the sensitivity of PM was higher than that of PR. Antigenic diversity of the S-layer proteins from 20 bacterial samples was analysed by ELISA with PM and PF1 (polyclonal antiserum aganist Aeromonas hydrophila TF7 S-layer protein) . The S-layer proteins were distinguishable from the extracellular toxin of the homogeneous strains in antigenic and biochemical characterization and the S-layer proteins were one of the main protective antigens.
%K Aeromonas hydrophila
%K S-layer protein
%K Purification
%K Biological activities
%K Antigenicity<br>嗜水气单胞菌
%K S蛋白
%K 纯化
%K 生物学活性
%K 抗原性
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=6D70FC6F56196D681AEDE2D2D8A9AF8F&yid=8A15F8B0AA0E5323&vid=933658645952ED9F&iid=0B39A22176CE99FB&sid=3986B25773CB6C30&eid=2DBBF45CC176713E&journal_id=0001-6209&journal_name=微生物学报&referenced_num=12&reference_num=10