A multi-approach study of the interaction of the Cu(II) and Ni(II) ions with alanylglycylhistamine, a mimicking pseudopeptide of the serum albumine N-terminal residue-Reference-Cited by-同舟云学术

A multi-approach study of the interaction of the Cu(II) and Ni(II) ions with alanylglycylhistamine, a mimicking pseudopeptide of the serum albumine N-terminal residue

Published:2005-05 Issue:5 Volume:99 Page:1182-1192
ISSN:0162-0134
Container-title:Journal of Inorganic Biochemistry
language:en
Short-container-title:Journal of Inorganic Biochemistry

Author:

Gizzi P.,Henry B.,Rubini P.,Giroux S.,Wenger E.

Publisher

Elsevier BV

Subject

Inorganic Chemistry,Biochemistry

Reference43 articles.

1. Specific structure–stability relations in metallopeptides

2. Copper-binding Properties of Bovine Serum Albumin and Its Amino-terminal Peptide Fragment

3. The State of Copper in Human Serum: Evidence for an Amino Acid-bound Fraction *

4. Evidence for albumin – Cu(II) – amino acid ternary complex

5. Characterization of the copper(II) and nickel(II) transport site of human serum albumin. Studies of copper(II) and nickel(II) binding to peptide 1-24 of human serum albumin by carbon-13 and proton NMR spectroscopy

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