Regeneration of enzyme activity by air oxidation of reduced subtilisin-modified ribonuclease.

作者: Edgar Haber , Christian B. Anfinsen

DOI: 10.1016/S0021-9258(18)64379-0

关键词:

摘要: Fully reduced bovine ribonuclease, a molecule which probably exists in random coil configuration (1, 2)) will, under the influence of molecular oxygen alone, oxidize to form an organized, enzymatically active product high yield (3, 4). This material seems indistinguishable on basis physical properties from native ribonuclease (RNase) . These observations suggest that information determining not only covalent structure, but also secondary and tertiary structure molecule, is contained amino acid sequence itself. It interest determine portions are most necessary for correct refolding. The reduction subsequent oxidation subtilisin-modified RNasei has, therefore, been studied attempt obtain at least partial answer this question. results described below indicate after removal 20 124 residues RNase chain, may be produced by fully derivative.

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