Biochemical and mass spectrometric characterization of soluble ecto-5'-nucleotidase from bull seminal plasma (Articolo in rivista)

Type
Label
  • Biochemical and mass spectrometric characterization of soluble ecto-5'-nucleotidase from bull seminal plasma (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Fini C., Talamo F., Cherri S., Coli M., Floridi A., Ferrara L. and Scaloni A. (2003)
    Biochemical and mass spectrometric characterization of soluble ecto-5'-nucleotidase from bull seminal plasma
    in Journal of Biochemistry (Tokyo)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Fini C., Talamo F., Cherri S., Coli M., Floridi A., Ferrara L. and Scaloni A. (literal)
Pagina inizio
  • 443 (literal)
Pagina fine
  • 451 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 372 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • Biochemical and mass spectrometric characterization of soluble ecto-5'-nucleotidase from bull seminal plasma (literal)
Abstract
  • Ecto-5'-nucleotidase (ecto-5'-NT) is a glycosylphosphatidylinositol-anchored membrane-bound protein that is ubiquitous in mammalian tissues. It is a target for a number of therapeutic drugs since increased levels of the enzyme correlate with various disease states. In this investigation, we describe the properties of a soluble ecto-5'-NT derived from bull seminal plasma. The protein was highly heterogeneous as demonstrated by chromatofocusing and two-dimensional PAGE. Sequencing analyses revealed a truncated polypeptide lacking the glycosylphospatidylinositol attachment site, suggesting that it is produced post-translationally by cleavage at Gln(547) and/or Phe(548). Heterogeneity was largely due to differential glycosylation, especially in the oligosaccharides linked to Asn(403). Significant differences in substrate specificity were observed between isoforms and, on the basis of molecular-modelling studies, were interpreted in terms of variable glycosylation causing steric hindrance of the substrate-binding site. Thus the soluble forms of ecto-5'-NT found in bull seminal plasma are unique both biochemically and structurally, and have a putative role in signalling interactions with spermatozoa following ejaculation and capacitation in the female reproductive tract. (literal)
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