title: Isolation of a thermostable enzyme catalyzing disulfide bond formation from the archaebacterium Sulfolobus solfataricus.
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.
authors.affiliation: Dipartimento di Chimica Organica e Biologica, Università di Napoli, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Guagliardi
authors.forename: L
authors.initials: L
authors.lastname: Cerchia
authors.forename: M
authors.initials: M
authors.lastname: De Rosa
authors.forename: M
authors.initials: M
authors.lastname: Rossi
authors.forename: S
authors.initials: S
authors.lastname: Bartolucci
mesh_terms: D000595:Amino Acid Sequence; D002384:Catalysis; D002853:Chromatography, Liquid; D004220:Disulfides / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004795:Enzyme Stability; D006358:Hot Temperature; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D050862:Oxidoreductases Acting on Sulfur Group Donors; D012260:Ribonucleases / Q000378:metabolism; D016944:Sulfolobus / Q000201:enzymology*
chemical_list: D004220:Disulfides; D010088:Oxidoreductases; D050862:Oxidoreductases Acting on Sulfur Group Donors; D012260:Ribonucleases