12 線毛をもたない Prevotella intermedia から分離精製した赤血球凝集因子の性状について (第440回大阪歯科学会例会)

概要

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Previous study have shown that partially purified hemagglutinin isolated from non-fimbriated Prevotella intermedia strain E18 can be further purified by arginine agarose and gel filtration. We characterized a purified hemagglutinin from this strain. Hemagglutination activity was sensitive to heat and proteolytic enzymes such as trypsin, chymotrypsin and protease. Addition of D-glucosamine, D-galactosamine, N-acetylneuraminic acid, L-lysine and L-arginine caused hemagglutination inhibition, suggesting that a common component in the above sugars and amino acid may be associated with receptors for hemagglutinin. Hemagglutination activity of the hemagglutinin was eliminated by anti-hemagglutinin serum. These results indicate that non-fimbriated hemagglutinin in this study is quite similar to a hemagglutinin derived from Prevotella intermedia fimbriae.
大阪歯科学会の論文
1995-04-25