Literature DB >> 3841168

Enzymes in ornithine-proline metabolic pathway in bovine lens.

T Shiono, S Hayasaka, S Hara, K Mizuno, T Matsuzawa, I Ishiguro.   

Abstract

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.

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Year:  1985        PMID: 3841168

Source DB:  PubMed          Journal:  Jpn J Ophthalmol        ISSN: 0021-5155            Impact factor:   2.447


  1 in total

1.  Acid hydrolases in the bovine lens epithelium.

Authors:  T Shiono
Journal:  Graefes Arch Clin Exp Ophthalmol       Date:  1988       Impact factor: 3.117

  1 in total

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