Weiss J M, Lembach K J, Boucek R J
Biochem J. 1981 Jan 15;194(1):229-39. doi: 10.1042/bj1940229.
Ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) has been purified from 3T3- and SV40-transformed 3T3 mouse fibroblasts by affinity chromatography, and the physicochemical properties of the two enzymes compared. Measured properties include molecular weight of the active species, subunit molecular weight and specific activity of the purified enzymes, kinetic parameters, thermostability, degradation rate in vivo and immunological cross-reactivity. Although crude extracts of the transformant possess more ornithine decarboxylase activity per mg of protein than the parent strain, there is no evidence for the appearance of an altered form of the enzyme in these cells. The results reported in the present paper indicate that the increased ornithine decarboxylase activity in the transformed cells is the result of higher enzyme biosynthesis de novo.
鸟氨酸脱羧酶(L-鸟氨酸羧基裂解酶,EC 4.1.1.17)已通过亲和色谱法从3T3细胞和SV40转化的3T3小鼠成纤维细胞中纯化出来,并对这两种酶的理化性质进行了比较。测定的性质包括活性物种的分子量、亚基分子量、纯化酶的比活性、动力学参数、热稳定性、体内降解率和免疫交叉反应性。尽管转化体的粗提取物每毫克蛋白质具有比亲代菌株更多的鸟氨酸脱羧酶活性,但没有证据表明这些细胞中出现了改变形式的酶。本文报道的结果表明,转化细胞中鸟氨酸脱羧酶活性的增加是从头合成更高酶量的结果。