Linked Life Data

2480789

Source:http://linkedlifedata.com/resource/pubmed/id/2480789

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
1990-1-19
pubmed:abstractText
The photochemical reactions of the bacteriocide bithionol (a known photoallergen in man) with soluble proteins and peptides, were investigated. Solutions of human serum albumin (HSA), human gamma-globulin, bovine insulin and poly-L-lysine were irradiated with ultraviolet light of wavelength 313 nm in the presence of [35S]-bithionol and the extent of photochemical (covalent) binding determined. HSA bound at least four molecules of bithionol per molecule of HSA. Bithionol was also found to bind to gamma-globulin to a similar extent; lower levels of binding were achieved with bovine insulin and poly-L-lysine. A bithionol-HSA photoadduct was treated with cyanogen bromide to determine the selectivity of binding. Fractionation after cyanogen bromide treatment showed that bithionol was bound to both major fragments of HSA, with a preference for the N-terminal region of the protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3879-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
The photochemical binding of bithionol to soluble proteins and peptides.
pubmed:affiliation
Department of Chemistry and Applied Chemistry, University of Wales, College of Cardiff, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't