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Macromolecularization of a tripeptide analogue of the Cu(II) binding site of human serum albumin: 2. Conformational and binding properties towards Cu(II) and Ni(II)ions of Gly-Gly-His derivatives of poly(l-lysine)

โœ Scribed by M.T. Foffani; S. Mammi; L. Michielin; E. Peggion


Book ID
119070040
Publisher
Elsevier Science
Year
1985
Tongue
English
Weight
752 KB
Volume
7
Category
Article
ISSN
0141-8130

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Macromolecularization of a tripeptide an
โœ L. Michielin; S. Mammi; E. Peggion ๐Ÿ“‚ Article ๐Ÿ“… 1983 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 227 KB ๐Ÿ‘ 1 views

The Cu(I1) binding site of human serum albumin is located on the N-terminal sequence Asp-Ala-His.l-4 It has been shown that the synthetic tripeptide Asp-Ala-His N-methylamide exhibits an affinity towards Cu(I1) ions even higher than that of serum albumin itself.5 In general, i t has been observed th