化脓放线菌产生的细胞外神经氨酸酶的特性研究。

Characterization of extracellular neuraminidase produced by Actinomyces pyogenes.

作者信息

Schaufuss P, Lämmler C

机构信息

Institut für Bakteriologie, Justus-Liebig-Universität Giessen.

出版信息

Zentralbl Bakteriol. 1989 May;271(1):28-35. doi: 10.1016/s0934-8840(89)80050-7.

DOI:10.1016/s0934-8840(89)80050-7

PMID:2765089

Abstract

Extracellular neuraminidase from Actinomyces pyogenes could be isolated by ammonium sulfate precipitation, ion exchange chromatography with DEAE cellulose and gel filtration on Ultrogel ACA 54. The purified enzyme had a molecular weight of approximately 50,000 Dalton, a pH optimum at pH 6.0, a temperature optimum at 55 degrees C and a Km value of 1.4 X 10(-4) mol/l with N-acetyl-neuraminlactose as substrate. Preparative isoelectric focussing of the culture supernatant revealed neuraminidase activity mainly at pH 6.5. The enzyme activity was not influenced by metalions or EDTA.

摘要

化脓放线菌的胞外神经氨酸酶可通过硫酸铵沉淀、用DEAE纤维素进行离子交换色谱以及在Ultrogel ACA 54上进行凝胶过滤来分离。纯化后的酶分子量约为50,000道尔顿，最适pH为6.0，最适温度为55℃，以N-乙酰神经氨酸乳糖为底物时的Km值为1.4×10⁻⁴mol/l。对培养上清液进行制备性等电聚焦显示，神经氨酸酶活性主要在pH 6.5处。酶活性不受金属离子或EDTA的影响。