Hölttä E
Biochim Biophys Acta. 1975 Aug 13;399(2):420-7. doi: 10.1016/0304-4165(75)90270-6.
Antiserum against ornithine decarboxylase (EC 4.1.1.17) was prepared in rabbits using purified ornithine decarboxylase from rat liver as the antigen. Immunoglobulins from the immune sera were covalently coupled to agarose by cyanogen bromide activation. With the aid of this immunoadsorbent against the enzyme it has been shown that following partial hepatectomy and growth hormone administration, the ornithine decarboxylase activity is elevated concomitantly with the increase in the immunoreactive enzyme protein. In addition, the rapid decay in ornithine decarboxylase activity in regenerating rat liver after cycloheximide injection is accompanied by a decrease in the immunoreactive protein. These results suggest that the activity of ornithine decarboxylase in rat liver is regulated through rapid changes in de novo synthesis and degradation of the enzyme protein.
以大鼠肝脏纯化的鸟氨酸脱羧酶为抗原，在兔体内制备了抗鸟氨酸脱羧酶（EC 4.1.1.17）抗血清。通过溴化氰活化，将免疫血清中的免疫球蛋白共价偶联到琼脂糖上。借助这种针对该酶的免疫吸附剂，已表明在部分肝切除和给予生长激素后，鸟氨酸脱羧酶活性伴随着免疫反应性酶蛋白的增加而升高。此外，注射放线菌酮后再生大鼠肝脏中鸟氨酸脱羧酶活性的快速下降伴随着免疫反应性蛋白的减少。这些结果表明，大鼠肝脏中鸟氨酸脱羧酶的活性是通过酶蛋白从头合成和降解的快速变化来调节的。
