PRIMARY STRUCTURE OF OVINE ALPHA(S1)-CASEINS - LOCALIZATION OF PHOSPHORYLATION SITES AND CHARACTERIZATION OF GENETIC-VARIANT-A, GENETIC-VARIANT-C AND GENETIC-VARIANT-D (Articolo in rivista)

Type
Label
  • PRIMARY STRUCTURE OF OVINE ALPHA(S1)-CASEINS - LOCALIZATION OF PHOSPHORYLATION SITES AND CHARACTERIZATION OF GENETIC-VARIANT-A, GENETIC-VARIANT-C AND GENETIC-VARIANT-D (Articolo in rivista) (literal)
Anno
  • 1995-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1017/S0022029900030983 (literal)
Alternative label
  • FERRANTI, P; MALORNI, A; NITTI, G; LAEZZA, P; PIZZANO, R; CHIANESE, L; ADDEO, F (1995)
    PRIMARY STRUCTURE OF OVINE ALPHA(S1)-CASEINS - LOCALIZATION OF PHOSPHORYLATION SITES AND CHARACTERIZATION OF GENETIC-VARIANT-A, GENETIC-VARIANT-C AND GENETIC-VARIANT-D
    in Journal of dairy research (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • FERRANTI, P; MALORNI, A; NITTI, G; LAEZZA, P; PIZZANO, R; CHIANESE, L; ADDEO, F (literal)
Pagina inizio
  • 281 (literal)
Pagina fine
  • 296 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 62 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 16 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Consiglio Nazionale delle Ricerche (CNR); CEINGE (literal)
Titolo
  • PRIMARY STRUCTURE OF OVINE ALPHA(S1)-CASEINS - LOCALIZATION OF PHOSPHORYLATION SITES AND CHARACTERIZATION OF GENETIC-VARIANT-A, GENETIC-VARIANT-C AND GENETIC-VARIANT-D (literal)
Abstract
  • The primary structures of ovine alpha(s1)-casein variants A, C and D (formerly called Welsh variant) were determined. Separation of variants from whole casein was achieved using a fast and reliable reversed-phase HPLC method. Extended structural characterization of the purified proteins using electrospray mass spectrometry, automated Edman degradation and peptide mapping by means of HPLC-fast atom bombardment-mass spectrometry demonstrated that the mature protein was a mixture of two molecular species that differed in the deletion of residues 141-148 and were therefore 199 and 191. residues long respectively. The 199 residue peptide chain, which accounted for similar to 80% of the entire translated alpha(s1)-casein, was as long as its caprine and bovine counterparts, and had a 98 and 89% degree of identity with those two proteins respectively. Nine serine residues (positions 12, 44, 46, 64 to 68 and 75) were fully phosphorylated in alpha(s1)-casein A, whereas Ser(115) and Ser(41) were phosphorylated by similar to 50 and similar to 20% respectively. The differences between the three genetic variants A, C and D were simple silent substitutions, which however involved the degree to which the protein was phosphorylated. Variant C differed from variant A in the substitution Ser(13) --> Pro(13) which determined the loss of the phosphate group on site 12 of the protein chain, SerP(12) --> Ser(12). A further substitution, SerP(68) --> Asn(68) caused the disappearance of both phosphate groups in the phosphorylated residues Ser(64) and Ser(66) in variant D; in this last casein variant there was no evidence of phosphorylation at Ser(41). (literal)
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