口腔レンサ球菌由来の菌体外グリコシダーゼについて

概要

論文の詳細を見る
Bacterial glycosidases that cleave carbohydrate components from salivary glycoproteins may be important in oral pathological conditions. The purpose of this study was to survey for the presence of extracellular glycosidases of some oral streptococci. Twenty-four strains of oral streptococci were grown in trypticase soy broth culture at 37℃ for 24 hours. The extracellular enzymes in the supernatant of culture were precipitated by the addition of 80% saturation of ammonium sulfate and then dissolved in phosphate buffer (pH 7.0). For the assay of α-L-fucosidase, porcine submaxillary glycoprotein (PSG) and/or ρ-nitrophenyl-α-L-fucoside (ρ-NPF) were used as substrates. Neuraminidase activity was determined using human plasma glycoprotein Fr. VI. Using corresponding ρ-nitrophenylglycosides, other glycosidase (β-galactosidase, β-N-acetylglucosaminidase, α-mannosidase) assays were performed. The free sugar and ρ-nitrophenol released, each was determined by the spectrophotometric method, respectively. Both activities of α-L-fucosidase against PSG and neuraminidase were found only in S. sanguis ATCC 10557 and S. mitis ATCC 9811. α-L-Fucosidase activity against ρ-NPF was not detectable in any strains. Several strains of S. sanguis possessed both β-galactosidase and β-N-acetylglucosaminidase activities. Only one strain in S. mutans tested produced β-N-acetylglucosaminidase. This study has demonstrated that bacterial glycosidases are produced by some oral streptococci. It is tempting to speculate that the streptococcal glycosidases may play a role in the degradation of salivary glycoproteins.
特定非営利活動法人日本歯周病学会の論文
1978-06-28

口腔レンサ球菌由来の菌体外グリコシダーゼについて

スポンサーリンク

概要

著者

関連論文

スポンサーリンク