一种针对鸟氨酸脱羧酶抗酶的大分子抑制剂。
A macromolecular inhibitor of the antizyme to ornithine decarboxylase.
作者信息
Fujita K, Murakami Y, Hayashi S
出版信息
Biochem J. 1982 Jun 15;204(3):647-52. doi: 10.1042/bj2040647.
Abstract
A macromolecular factor that inhibits the activity of the antizyme to ornithine decarboxylase (ODC) was found in rat liver extracts. The factor, 'antizyme inhibitor', was heat-labile, non diffusable and of similar molecular size to ODC. The antizyme inhibitor re-activated ODC that had been inactivated by antizyme, apparently by replacing ODC in a complex with antizyme. Therefore the antizyme inhibitor can be used to assay the amount of inactive ODC-antizyme complex formed in vitro. When assayed by this method, the complex was shown to be eluted before ODC from a Sephadex G-100 column. Significant increase in ODC activity was observed when the antizyme inhibitor was added to crude liver extracts from rats that had been injected with 1,3-diaminopropane to cause decay of ODC activity, suggesting the presence of inactive ODC-antizyme complex in the extracts.
摘要
在大鼠肝脏提取物中发现了一种抑制抗鸟氨酸脱羧酶（ODC）抗酶活性的大分子因子。该因子“抗酶抑制剂”对热不稳定，不可扩散，且分子大小与ODC相似。抗酶抑制剂能使已被抗酶失活的ODC重新激活，显然是通过取代与抗酶形成复合物的ODC来实现的。因此，抗酶抑制剂可用于测定体外形成的无活性ODC - 抗酶复合物的量。用这种方法测定时，该复合物在Sephadex G - 100柱上比ODC先被洗脱。当将抗酶抑制剂添加到已注射1,3 - 二氨基丙烷致使ODC活性衰减的大鼠肝脏粗提物中时，观察到ODC活性显著增加，这表明提取物中存在无活性的ODC - 抗酶复合物。
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