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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
