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Isolation of a thermostable enzyme catalyzing disulfide bond formation from the archaebacterium Sulfolobus
A Guagliardi1, L Cerchia, M De Rosa
1Dipartimento di Chimica Organica e Biologica, Università di Napoli, Italy.
FEBS Letters
|May 25, 1992
Abstract:
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.