Repozytorium
Wyszukaj
Kolekcje
Inne
Binding ability of Cu+2 ions by opiate-like fragments of bovine casein.
Autorzy
Rok wydania
1997
Czasopismo
Journal of Inorganic Biochemistry
Numer woluminu
66
Strony
19-22
DOI
10.1016/s0162-0134(96)00147-x
Kolekcja
Język
Angielski
Typ publikacji
Artykuł
The coordination modes of Cu(II) to alpha-casein (90-95) and alpha-casein (90-96) peptides with opioid activity isolated from pepsin hydrolisates of alpha-casein were investigated by means of electron paramagnetic resonance, absorption, and circular dichroism spectroscopy and potentiometry. The results allow the identification of the complex species involved and the attribution of the spectral data set to the various complex structures. According to the spectroscopic data, a phenolate side-chain of Tyr residue belonging to the Gly-Tyr-Leu or Gly-Tyr-Leu-Gln fragment of the peptides is involved in the metal coordination in a complex which is a minor species at neutral pH range.
Adres publiczny
https://doi.org/10.1016/s0162-0134(96)00147-x
Strona internetowa wydawcy
Podobne publikacje
Unusual binding ability of vancomycin towards Cu2+ ions.
Świątek Magdalena, Valensin Daniela, Migliorini Caterina, Gaggelli Elena, Valensin Gianni, Jeżowska-Bojczuk Małgorzata
Effect of α-hydroxymethylserine residue on binding ability of oligopeptides to Cu2+ ions.
Kowalik-Jankowska Teresa, Stasiak M., Leplawy Mirosław T., Kozłowski Henryk
Unusual gain in the coordination ability of vasopressin-like peptides towards Cu2+ ions by insertion of the highly hydrophobic side chain.
Chruścińska E., Derdowska I., Kozłowski Henryk, Lammek B., Łuczkowski Marek, Ołdziej S., Świątek-Kozłowska Jolanta