Thermostable beta-galactosidase from the archaebacterium Sulfolobus solfataricus. Purification and properties. (Articolo in rivista)

Type
Label
  • Thermostable beta-galactosidase from the archaebacterium Sulfolobus solfataricus. Purification and properties. (Articolo in rivista) (literal)
Anno
  • 1990-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1111/j.1432-1033.1990.tb15308.x (literal)
Alternative label
  • F.M. Pisani, R. Rella, C. Raia, C. Rozzo, R. Nucci, A. Gambacorta, M. De Rosa, M. Rossi. (1990)
    Thermostable beta-galactosidase from the archaebacterium Sulfolobus solfataricus. Purification and properties.
    in European journal of biochemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • F.M. Pisani, R. Rella, C. Raia, C. Rozzo, R. Nucci, A. Gambacorta, M. De Rosa, M. Rossi. (literal)
Pagina inizio
  • 321 (literal)
Pagina fine
  • 328 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 187 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 8 (literal)
Note
  • PubMe (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biochimica delle Proteine ed Enzimologia, Consiglio Nazionale delle Ricerche, Napoli, Italia Istituto per lo Studio delle Molecole di Interesse Biologico, Consiglio Nazionalc delle Riccrche, Napoli, Italia (literal)
Titolo
  • Thermostable beta-galactosidase from the archaebacterium Sulfolobus solfataricus. Purification and properties. (literal)
Abstract
  • A thermophilic and thermostable beta-galactosidase activity was purified to homogeneity from crude extracts of the archaebacterium Sulpholobus solfataricus, by a procedure including ion-exchange and affinity chromatography. The homogeneous enzyme had a specific activity of 116.4 units/mg at 75 °C with o-nitrophenyl P-galactopyranoside as substrate. Molecular mass studies demonstrated that the S. solfataricus beta-galactosidase was a tetramer of 240 Ifr S kDa composed of similar or identical subunits. Comparison of the amino acid composition of beta-galactosidase from S. solfataricus with that from Escherichia coli revealed a lower cysteine content and a lower Arg/Lys ratio in the thermophilic enzyme. A rabbit serum, raised against the homogeneous enzyme did not crossreact with beta-galactosidase from E. coli. The enzyme, characterized for its reaction requirements and kinetic properties, showed a thermostability and thermophilicity notably greater than those reported for beta-galactosidases from other mesophilic and thermophilic sources. (literal)
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