用抗酶和亲和标记法测定小鼠肾脏和大鼠肝脏鸟氨酸脱羧酶的催化中心活性相同。
Identical catalytic-centre activity for mouse kidney and rat liver ornithine decarboxylases as determined with antizyme and affinity labelling.
作者信息
Marumo M, Matsufuji S, Murakami Y, Hayashi S
机构信息
Department of Nutrition, Jikei University School of Medicine, Tokyo, Japan.
出版信息
Biochem J. 1988 Feb 1;249(3):907-10. doi: 10.1042/bj2490907.
Abstract
Since the catalytic-centre activity of mouse kidney ornithine decarboxylase (ODC) has been assumed to be twice as high as that of rat liver ODC, we compared relative catalytic-centre activity of the two enzymes by titration with antizyme, which inhibits ODC by stoichiometric binding. In either a crude or a purified state, both enzymes were inhibited by rat liver antizyme to the same extent, indicating that they have nearly identical catalytic-centre activities. This conclusion was supported by comparison of affinity labelling of the enzymes with alpha-difluoromethyl[14C]ornithine.
摘要
由于假定小鼠肾脏鸟氨酸脱羧酶（ODC）的催化中心活性是大鼠肝脏ODC的两倍，我们通过用抗酶滴定来比较这两种酶的相对催化中心活性，抗酶通过化学计量结合来抑制ODC。无论是粗提状态还是纯化状态，两种酶都被大鼠肝脏抗酶以相同程度抑制，这表明它们具有几乎相同的催化中心活性。用α-二氟甲基[14C]鸟氨酸对酶进行亲和标记的比较支持了这一结论。
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Affinity labeling of purified ornithine decarboxylase by alpha-difluoromethylornithine.α-二氟甲基鸟氨酸对纯化的鸟氨酸脱羧酶的亲和标记
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