Hayano S, Tanaka A
J Bacteriol. 1969 Mar;97(3):1328-33. doi: 10.1128/jb.97.3.1328-1333.1969.
A group of enzymes were prepared from the culture fluids of streptococci belonging to groups A, B, C, G, and L, and from a strain of Streptococcus sanguis. These streptococcal enzymes (designated St-sialidases) released a substance shown to belong to the sialic acid group from the specific substrate BSM-St, a sialomucoid prepared from bovine submaxillary gland. They were inactive on N-acetylneuramin lactose prepared from bovine colustrum and on a sialomucoid prepared from bovine submaxillary mucin, whereas these substances are susceptible to sialidases produced by group K streptococci and by Vibrio cholerae. Some of the St-sialidases were markedly activated by divalent cations, but others showed little response. The heat stability of the enzymes produced by the different strains varied. The optimal pH was between 5.5 and 6.5 with acetate buffer and was about 7 with phosphate buffer. K(m) values were determined for the St-sialidases with BSM-St as substrate.
从A、B、C、G和L组链球菌以及一株血链球菌的培养液中制备了一组酶。这些链球菌酶(称为St-唾液酸酶)能从特定底物BSM-St(一种从牛下颌腺制备的唾液粘蛋白)中释放出一种被证明属于唾液酸基团的物质。它们对从牛初乳制备的N-乙酰神经氨酸乳糖以及从牛下颌粘蛋白制备的唾液粘蛋白无活性,而这些物质易受K组链球菌和霍乱弧菌产生的唾液酸酶作用。一些St-唾液酸酶被二价阳离子显著激活,但其他的反应很小。不同菌株产生的酶的热稳定性各不相同。在醋酸盐缓冲液中,最佳pH值在5.5至6.5之间,在磷酸盐缓冲液中约为7。以BSM-St为底物测定了St-唾液酸酶的米氏常数。