Persson L
Acta Physiol Scand. 1977 Aug;100(4):424-9. doi: 10.1111/j.1748-1716.1977.tb05966.x.
In enzymic preparations from mouse kidney stimulated with the anabolic steroid Durabolin (nandrolone phenpropionate) lysine and ornithine were shown to inhibit the decarboxylation of each other competitively. The Michaelis constants for the decarboxylations were approximately equal to the inhibition constants of the two amino acids. The pH optima of the decarboxylation of lysine and ornithine were found to be identical. Chromatographic studies of the enzyme preparation on a Sephadex G-150 Superfine column did not bring about a separation of the two enzyme activities. The ratio of the decarboxylating activities was practically the same during the elution. Lysine decarboxylating activity was also shown to be present in growth hormone stimulated rat liver. The results are in agreement with the assumption that the decarboxylation of lysine and ornithine is carried out by the same enzyme.
在用合成代谢类固醇大力补（苯丙酸诺龙）刺激的小鼠肾脏酶制剂中，赖氨酸和鸟氨酸被证明相互竞争性抑制脱羧作用。脱羧反应的米氏常数大约等于这两种氨基酸的抑制常数。发现赖氨酸和鸟氨酸脱羧反应的最适pH值相同。在Sephadex G - 150 Superfine柱上对酶制剂进行色谱研究，未能分离出两种酶活性。洗脱过程中脱羧活性的比例实际上是相同的。生长激素刺激的大鼠肝脏中也显示存在赖氨酸脱羧活性。这些结果与赖氨酸和鸟氨酸的脱羧由同一种酶进行的假设一致。
