@article{oai:nagasaki-u.repo.nii.ac.jp:00025145,
 author = {江原, 雅彦 and 石橋, 美雅子 and 一瀬, 休生 and FERNANDES, Sueli A.},
 issue = {2},
 journal = {熱帯医学 Tropical medicine},
 month = {Jun},
 note = {D-mannose sensitiveなHA活性をもつS. adelaideとS. agonaの2株を教室保存株から選定し,それぞれの線毛を精製した.精製に関してはKorhonen, T. K らの方法に準じて行った.線毛の幅は約5-7nmでaxial holeを有し, subunitの分子量は21,000 Daで,アミノ酸分析の結果,疎水性アミノ酸の含量は約32%であった.赤血球凝集試験ではWhole cell(fimbriate phase)では高い凝集能を示したが,精製した線毛は全く凝集能を示さなかった.また,この精製した線毛を用いて家兎を免疫し,得られた抗体は線毛のsubunitは認識せず,native fimbriaeのみを認識した.このことは線毛の抗原決定基には蛋白質の三次構造が何らかの役割を担っていることを示唆した., Fimbriae from S. adelaide and S. agona were purified and characterized. These fimbriae were 5 to 7 nm in diameter. The molecular weight of fimbrial subunits was 21,000 Da as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and this molecular weight was similar to that of S. typhimurium fimbriae (Mr. 22,000) (Korhonen et al., 1980). Hydrophobic amino acids of the fimbriae comprised 32% of the total amino acids. Whole cells agglutinated chicken erythrocytes but purified fimbriae did not have haemagglutination activity. Antibodies raised against the native fimbriae recognized only native fimbriae but not fimbrial subunits. Both fimbriae shared common antigenic determinants exposed on both sides of the fiber., 熱帯医学 Tropical medicine 30(2). p93-103, 1988},
 pages = {93--103},
 title = {S. adelaideとS. agonaの線毛の精製,及びその性状},
 volume = {30},
 year = {1988}
}