Marumo M, Matsufuji S, Murakami Y, Hayashi S
Department of Nutrition, Jikei University School of Medicine, Tokyo, Japan.
Biochem J. 1988 Feb 1;249(3):907-10. doi: 10.1042/bj2490907.
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.
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。
