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Specific interactions of bovine and human beta-casomorphin-7 with Cu(II) ions

Chruscinska, Elzebieta and Olczak, Jacek and Zabrocki, Janusz and Dyba, Marcin and Micera, Giovanni and Sanna, Daniele and Kozlowski, Henryk (1998) Specific interactions of bovine and human beta-casomorphin-7 with Cu(II) ions. Journal of Inorganic Biochemistry, Vol. 69 (1-2), p. 91-95. ISSN 0162-0134. Article.

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DOI: 10.1016/S0162-0134(97)10025-3


Complex formation between Cu(II) and human and bovine β-casomorphin heptapeptides, Tyr-Pro-Phe-Val-Glu-Pro-Ile and Tyr-Pro-Phe-Pro-Gly-Pro-Ile, respectively, was investigated by pH potentiometry and spectroscopic (CD, EPR and electronic absorption) techniques. The results showed the critical impact of Pro residues on the complex equilibria formed. The presence of the Pro residue at the second position leads to formation of very stable dimeric species in which two metal ions co-ordinate to N-terminal {NH2,C=O} binding sites of one peptide molecule and the deprotonated phenolic oxygen of the second ligand molecule. The presence of two additional hydrophobic residues on the C-terminal makes heptapeptide molecule much more effective ligand than its pentapeptide N-terminal fragment.

Item Type:Article
ID Code:1412
Uncontrolled Keywords:Human, bovine, β-casomorphin-7
Subjects:Area 03 - Scienze chimiche > CHIM/03 Chimica generale e inorganica
Divisions:001 Università di Sassari > 01 Dipartimenti > Chimica
Publisher:Elsevier Science
Additional Information:Pubblicato online il 20 aprile 1999.
Deposited On:18 Aug 2009 10:05

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