1. A purification procedure for a thioredoxin from the extremophilic archaeon Sulfolobus solfataricus is described. 2. The thioredoxin is active in the dithiothreitol-dependent reduction of insulin disulfide bonds. 3. The thioredoxin is a monomer of 24,800 Da; it is an acidic protein with a pi of 4.5. 4. The protein is stable to heating for 3 hr at 90°C. 5. The amino acid composition of S. solfataricus thioredoxin is reported.

Isolation of a thioredoxin from the extreme thermophilic Archaebacterium Sulfolobus solfataricus / Guagliardi, A.; Nobile, V.; Bartolucci, Simonetta; Rossi, M.. - In: JOURNAL OF BIOCHEMISTRY. - ISSN 0021-924X. - STAMPA. - 26:(1994), pp. 375-380. [10.1016/0020-711X(94)90057-4]

Isolation of a thioredoxin from the extreme thermophilic Archaebacterium Sulfolobus solfataricus.

GUAGLIARDI A.;BARTOLUCCI, SIMONETTA;
1994

Abstract

1. A purification procedure for a thioredoxin from the extremophilic archaeon Sulfolobus solfataricus is described. 2. The thioredoxin is active in the dithiothreitol-dependent reduction of insulin disulfide bonds. 3. The thioredoxin is a monomer of 24,800 Da; it is an acidic protein with a pi of 4.5. 4. The protein is stable to heating for 3 hr at 90°C. 5. The amino acid composition of S. solfataricus thioredoxin is reported.
1994
Isolation of a thioredoxin from the extreme thermophilic Archaebacterium Sulfolobus solfataricus / Guagliardi, A.; Nobile, V.; Bartolucci, Simonetta; Rossi, M.. - In: JOURNAL OF BIOCHEMISTRY. - ISSN 0021-924X. - STAMPA. - 26:(1994), pp. 375-380. [10.1016/0020-711X(94)90057-4]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/132265
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