来自猕猴肝脏的硫氰酸酶。I. 纯化及一些物理特性。

Rhodanese from Cercopithecus aethiops (vervet monkey) liver. I. Purification and some physical characteristics.

作者信息

Janse van Rensburg L, Schabort J C

出版信息

Int J Biochem. 1984;16(5):539-46. doi: 10.1016/0020-711x(84)90172-1.

Abstract

Rhodanese (thiosulphate sulphurtransferase , EC 2.8.1.1.) from Cercopithecus aethiops (vervet monkey) liver has been isolated and purified by means of extraction, ammoniumsulphate and pH fractionation, anion-exchange chromatography, Sephacryl S-300 gel chromatography and cation-exchange chromatography. A yield of about 10% pure enzyme with a specific activity of 242 U/mg protein corresponding to a purification factor of 523 was obtained. The enzyme was physically characterized and its homogeneity determined by electrophoretic studies and gel chromatography. The rhodanese enzyme has a molecular weight of 37,000 daltons, a D020 ,w value of 7.6 X 10(-7) cm2 sec-1, a Stokes radius (molecular size) of 2.75 X 10(-7) cm and a frictional ratio of 1.071.

摘要

已通过提取、硫酸铵和pH分级分离、阴离子交换色谱、Sephacryl S - 300凝胶色谱和阳离子交换色谱，从长尾黑颚猴（绿猴）肝脏中分离并纯化了硫氰酸酶（硫代硫酸盐硫转移酶，EC 2.8.1.1.）。获得了约10%的纯酶，其比活性为242 U/mg蛋白质，纯化因子为523。通过电泳研究和凝胶色谱对该酶进行了物理表征并确定了其纯度。硫氰酸酶的分子量为37,000道尔顿，D020,w值为7.6×10(-7) cm2 sec-1，斯托克斯半径（分子大小）为2.75×10(-7) cm，摩擦比为1.071。