Shiono T, Hayasaka S, Hara S, Mizuno K, Matsuzawa T, Ishiguro I
Jpn J Ophthalmol. 1985;29(3):305-9.
Various enzyme activities related to ornithine metabolism were studied using bovine lenses, ie, ornithine ketoacid transaminase, delta-1-pyrroline-5-carboxylate reductase, and delta-1-pyrroline-5-carboxylate dehydrogenase. Ornithine ketoacid transaminase activity was found in the lens epithelium; delta-1-pyrroline-5-carboxylate reductase activity was high in both lens epithelium and cortex plus nucleus; delta-1-pyrroline-5-carboxylate dehydrogenase activity was negligible in either lens epithelium or cortex plus nucleus. These results suggest that in the bovine lens ornithine is converted to proline by the cooperative action of ornithine ketoacid transaminase and delta-1-pyrroline-5-carboxylate reductase.
利用牛晶状体研究了与鸟氨酸代谢相关的各种酶活性，即鸟氨酸酮酸转氨酶、δ-1-吡咯啉-5-羧酸还原酶和δ-1-吡咯啉-5-羧酸脱氢酶。在晶状体上皮中发现了鸟氨酸酮酸转氨酶活性；δ-1-吡咯啉-5-羧酸还原酶活性在晶状体上皮以及皮质加核中均较高；δ-1-吡咯啉-5-羧酸脱氢酶活性在晶状体上皮或皮质加核中均可忽略不计。这些结果表明，在牛晶状体中，鸟氨酸通过鸟氨酸酮酸转氨酶和δ-1-吡咯啉-5-羧酸还原酶的协同作用转化为脯氨酸。
