Włodek L, Ostrowski W S
Acta Biochim Pol. 1982;29(1-2):121-33.
3-Mercaptopyruvate sulphurtransferase (EC 2.8.1.2) was isolated from rat erythrocytes and purified to apparent homogeneity. On disc electrophoresis and isoelectric focusing the enzyme showed microheterogeneity; four enzymatically active microzones of isoelectric points ranging from 5.5 to 7.5, resistant to neuraminidase treatment were detected. The molecular mass of the enzyme determined by the density gradient ultracentrifugation, gel filtration and sodium dodecyl sulphate polyacrylamide-gel electrophoresis was found to be about 36,000. The enzyme is a sialoprotein composed of 219 amino acid and 38 carbohydrate residues. Kinetic parameters of 3-mercaptopyruvate sulphurtransferase from rat erythrocytes were similar to those found for the enzymes isolated from rat liver and Escherichia coli. The purified enzyme was very unstable; spontaneous inactivation could be partly prevented by glycerol (1:5, v/v).
从大鼠红细胞中分离出3-巯基丙酮酸硫转移酶（EC 2.8.1.2）并纯化至表观同质。在圆盘电泳和等电聚焦中，该酶表现出微不均一性；检测到四个等电点范围为5.5至7.5的酶活性微区，对神经氨酸酶处理具有抗性。通过密度梯度超速离心、凝胶过滤和十二烷基硫酸钠聚丙烯酰胺凝胶电泳测定的酶分子量约为36,000。该酶是一种由219个氨基酸和38个碳水化合物残基组成的唾液酸糖蛋白。大鼠红细胞中3-巯基丙酮酸硫转移酶的动力学参数与从大鼠肝脏和大肠杆菌中分离出的酶相似。纯化后的酶非常不稳定；甘油（1:5，v/v）可部分防止其自发失活。
