Bacterial expression of Scapharca dimeric hemoglobin: a simple model system for investigating protein cooperatively. (Articolo in rivista)

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Label
  • Bacterial expression of Scapharca dimeric hemoglobin: a simple model system for investigating protein cooperatively. (Articolo in rivista) (literal)
Anno
  • 1995-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1093/protein/8.6.593 (literal)
Alternative label
  • Summerford CM, Pardanani A, Betts AH, Poteete AR, Colotti G, Royer WE Jr. (1995)
    Bacterial expression of Scapharca dimeric hemoglobin: a simple model system for investigating protein cooperatively.
    in Protein engineering (Print); OXFORD UNIV PRESS, OXFORD OX2 6DP, (Regno Unito)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Summerford CM, Pardanani A, Betts AH, Poteete AR, Colotti G, Royer WE Jr. (literal)
Pagina inizio
  • 593 (literal)
Pagina fine
  • 599 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 8 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 7 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 6 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • UNIV MASSACHUSETTS,MED CTR,PROGRAM MOLEC MED,WORCESTER,MA 01605 UNIV MASSACHUSETTS,MED CTR,DEPT BIOCHEM & MOLEC BIOL,WORCESTER,MA 01605 UNIV MASSACHUSETTS,MED CTR,DEPT MOLEC GENET & MICROBIOL,WORCESTER,MA 01605 UNIV ROMA LA SAPIENZA,DEPT BIOCHEM SCI, CNR,CTR BIOL MOLEC,I-00185 ROME,ITALY (literal)
Titolo
  • Bacterial expression of Scapharca dimeric hemoglobin: a simple model system for investigating protein cooperatively. (literal)
Abstract
  • Recombinant Scapharca homodimeric hemoglobin has been expressed at high levels from a synthetic gene in Escherichia coli. Addition of the heme precursor delta-aminolevulinic acid to the expression culture results in a considerable increase in the yield of soluble hemoglobin. The recombinant hemoglobin exhibits cooperative oxygen binding properties indistinguishable from native protein. Crystals of the recombinant protein, like those of native hemoglobin, diffract to high resolution which will allow functional studies of site-directed mutants to be correlated with detailed structural analyses. (literal)
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