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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1977-2-24
|
| pubmed:abstractText |
The reaction of the radical anion -(SCN)2-, produced during pulse radilysis of aqueous KCNS solutions, have been used to study the binding of a range of alkyl sulphates to bovine (BSA) and human (HSA) serum albumin. At neutral pH, -(SCN)2- reacts chiefly with trytophan residues. Approximately ten high-affinity binding sites are detectable for compounds of chain length greater than C7. The results are interpreted in terms of a model in which one hydrophobic region in the protein, containing the tryptophan residues, can accommodate the ten ligand molecules. Electrostatic interactions with positively-charged groups surrounding the hydrophobic area are also involved in binding.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0020-7616
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
30
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
449-57
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading | |
| pubmed:year |
1976
|
| pubmed:articleTitle |
Investigation of the interaction of alkyl sulphates with serum albumin using the thiocyanate radical ion (SCN)2.
|
| pubmed:publicationType |
Journal Article,
In Vitro
|