Murakami Y, Matsufuji S, Nishiyama M, Hayashi S
Department of Nutrition, Jikei University School of Medicine, Tokyo, Japan.
Biochem J. 1989 May 1;259(3):839-45. doi: 10.1042/bj2590839.
Antizyme inhibitor was highly purified from rat liver by using affinity chromatography. It has some structural resemblance to ornithine decarboxylase (ODC), as judged from Mr, immunoreactivity and reversible binding with antizyme. However, unlike hepatic amounts of ODC and ODC-antizyme complex, that of antizyme inhibitor did not show much fluctuation upon putrescine treatment, whereas it decreased as rapidly as ODC decay in the presence of cycloheximide. These results suggested that antizyme inhibitor is an independent regulatory protein rather than a derivative of ODC. Changes in hepatic amounts of antizyme inhibitor, antizyme and ODC upon feeding suggested that antizyme inhibitor may play a role in ODC regulation by trapping antizyme and thereby suppressing ODC degradation. A monoclonal antibody to rat liver antizyme inhibitor was obtained. This antibody was shown to be utilizable for a simple assay of antizyme-inhibitor activity in tissue extracts.
通过亲和层析法从大鼠肝脏中高度纯化出抗酶抑制剂。从分子量、免疫反应性以及与抗酶的可逆结合判断,它与鸟氨酸脱羧酶(ODC)在结构上有一些相似之处。然而,与肝脏中ODC和ODC - 抗酶复合物的量不同,抗酶抑制剂的量在腐胺处理后没有太大波动,而在环己酰亚胺存在下,它与ODC降解一样迅速减少。这些结果表明,抗酶抑制剂是一种独立的调节蛋白,而非ODC的衍生物。喂食后肝脏中抗酶抑制剂、抗酶和ODC量的变化表明,抗酶抑制剂可能通过捕获抗酶从而抑制ODC降解,在ODC调节中发挥作用。获得了针对大鼠肝脏抗酶抑制剂的单克隆抗体。该抗体可用于简单检测组织提取物中的抗酶抑制剂活性。