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pubmed-article:17516096pubmed:abstractTextThe conditional stability constant at pH 7.4 for Cu(II) binding at the N-terminal site (NTS) of human serum albumin (HSA) was determined directly by competitive UV-vis spectroscopy titrations using nitrilotriacetic acid (NTA) as the competitor in 100 mM NaCl and 100 mM N-(2-hydroxyethyl)piperazine-N'-ethanesulfonic acid (Hepes). The log Kc (NTS) value of 12.0 +/- 0.1 was determined for HSA dissolved in 100 mM NaCl. A false log log Kc (NTS) (c) value of 11.4 +/- 0.1 was obtained in the 100 mM Hepes buffer, owing to the formation of a ternary Cu(NTA)(Hepes) complex. The impact of the picomolar affinity of HSA for Cu(II) on the availability of these ions in neurodegenerative disorders is briefly discussed.lld:pubmed
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pubmed-article:17516096pubmed:year2007lld:pubmed
pubmed-article:17516096pubmed:articleTitleHuman serum albumin coordinates Cu(II) at its N-terminal binding site with 1 pM affinity.lld:pubmed
pubmed-article:17516096pubmed:affiliationInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawi?skiego 5a, 02-106 Warsaw, Poland.lld:pubmed
pubmed-article:17516096pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:17516096pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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