唾液酸酶链霉菌的纯化与特性分析。
Purification and characterization of Streptomyces sialidases.
作者信息
Kunimoto S, Aoyagi T, Takeuchi T, Umezawa H
出版信息
J Bacteriol. 1974 Aug;119(2):394-400. doi: 10.1128/jb.119.2.394-400.1974.
Some strains of Streptomyces produce sialidases. Two sialidases were purified over 1,000-fold from a culture filtrate of two Streptomyces species. They had the same properties in molecular weight, behavior to ions and other reagents, and substrate specificity. They showed very small differences in kinetic properties, pH optima, and heat stability. These Streptomyces sialidases differed markedly from Clostridium perfringens sialidase in molecular weight, p-chloromercuribenzoate sensitivity, and substrate specificity. Approximate molecular weights of the sialidases from Streptomyces and C. perfringens were 32,000 and 57,000, respectively. p-Chloromercuribenzoate (10(-3) M) caused complete inhibition of C. perfringens sialidase but not of Streptomyces sialidases.
一些链霉菌菌株会产生唾液酸酶。从两种链霉菌的培养滤液中纯化出了两种唾液酸酶，纯化倍数超过1000倍。它们在分子量、对离子及其他试剂的反应以及底物特异性方面具有相同的特性。它们在动力学特性、最适pH值和热稳定性方面表现出非常小的差异。这些链霉菌唾液酸酶在分子量、对对氯汞苯甲酸的敏感性和底物特异性方面与产气荚膜梭菌唾液酸酶有显著差异。链霉菌和产气荚膜梭菌唾液酸酶的近似分子量分别为32,000和57,000。10⁻³ M的对氯汞苯甲酸会完全抑制产气荚膜梭菌唾液酸酶，但不会抑制链霉菌唾液酸酶。
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