来自假单胞菌属菌株C12B的芳基硫酸酯酶：纯化至同质、免疫分析及物理性质
Arylsulfatase from Pseudomonas sp. strain C12B: purification to homogeneity, immunological analysis, and physical properties.
作者信息
George J R, Fitzgerald J W
出版信息
J Bacteriol. 1981 Mar;145(3):1428-31. doi: 10.1128/jb.145.3.1428-1431.1981.
Abstract
Arylsulfatase was purified 219-fold from Pseudomonas sp. strain C12B. The final preparation was homogeneous by electrophoretic and immunological analysis. The enzyme is a monomer of molecular weight about 51,000, with a Stokes radius of 3.0 X 10(-7) cm, a frictional ratio of 1.2, and a sedimentation coefficient of 4.1S.
摘要
芳基硫酸酯酶从假单胞菌属菌株C12B中纯化了219倍。最终制剂通过电泳和免疫分析显示为均一的。该酶是一种分子量约为51,000的单体，斯托克斯半径为3.0×10⁻⁷厘米，摩擦比为1.2，沉降系数为4.1S。
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