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

[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.

[学科分类] 生物化学/生物物理

[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