Anosike E O, Jack A S
Enzyme. 1982;27(1):33-9. doi: 10.1159/000459019.
Rhodanese (EC 2.8.1.1) has been partially purified from guinea pig and rat kidneys. The specific activities of the preparations were 1.23 and 0.44 mumol of product formed per minute per milligramme of enzyme protein. The guinea pig kidney enzyme had Km values of 14.2 and 31.5 mmol/l for cyanide and thiosulphate, respectively, while for the rat kidney enzyme, these values were 5.7 and 24.4 mmol/l, respectively. The temperature optimum of the enzyme from the two sources was 20 degrees C, while the pH optima were between 7.5 and 8.0. The molecular weight of the guinea pig kidney enzyme was 37,000, while that of the rat was 32,000. The difference in the levels of rhodanese activity in the two types of rodents is discussed in relation to their dietary habits.
硫氰酸酶(EC 2.8.1.1)已从豚鼠和大鼠肾脏中部分纯化出来。制备物的比活性分别为每分钟每毫克酶蛋白形成1.23和0.44微摩尔产物。豚鼠肾脏酶对氰化物和硫代硫酸盐的Km值分别为14.2和31.5毫摩尔/升,而大鼠肾脏酶的这些值分别为5.7和24.4毫摩尔/升。两种来源的酶的最适温度为20℃,最适pH值在7.5至8.0之间。豚鼠肾脏酶的分子量为37000,而大鼠的为32000。根据两种啮齿动物的饮食习惯,讨论了它们硫氰酸酶活性水平的差异。