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.
Isolation of a thermostable enzyme catalyzing disulfide bond formation from the archaebacterium Sulfolobus solfataricus / Guagliardi, A; Cerchia, L; DE ROSA, M; Rossi, M; Bartolucci, Simonetta. - In: FEBS LETTERS. - ISSN 0014-5793. - STAMPA. - 303:1(1992), pp. 27-30. [10.1016/0014-5793(92)80470-2]
Isolation of a thermostable enzyme catalyzing disulfide bond formation from the archaebacterium Sulfolobus solfataricus.
GUAGLIARDI A;BARTOLUCCI, SIMONETTA
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.File in questo prodotto:
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