Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-7-27
pubmed:abstractText
The 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0949-8257
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
913-8
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Human serum albumin coordinates Cu(II) at its N-terminal binding site with 1 pM affinity.
pubmed:affiliation
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawi?skiego 5a, 02-106 Warsaw, Poland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't