Isolation of a thermostable enzyme catalyzing disulfide bond formation from the archaebacterium Sulfolobus solfataricus

FEBS Letters

Cerchia, Laura²  Bartolucci, Simonetta²  Rossi, Mosè¹  De Rosa, Mario²  Guagliardi, Annamaria² 

[1] Istituto di Biochimica delle Proteine ed Enzimologia, C.N.R., Via Marconi 10, 80125 Napoli, Italy;Dipartimento di Chimica Organica e Biologica, Università di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy

关键词: Archaebacteria;    Disulfide bond formation;    Thermostable enzyme;    EDTA;    ethylene diamine tetraacetic acid;    DTNB;    5;    5′-dithio-bis-nitrobenzoic acid;    DTT;    dithiothreitol;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/0014-5793(92)80470-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A disulfide bond-forming enzyme was purified from the cytosol of the archaebacterium Sulfolobus solfataricus, strain MT-4. The enzyme, assayed by its ability to oxidize and reactivate reductively denatured ribonuclease A, had a small molecular size and displayed a high thermostability. The N-terminal amino acid sequence is reported.

【 授权许可】

Unknown