http://www.cnr.it/ontology/cnr/individuo/prodotto/ID213490
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
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- 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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- Autore CNR
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