Linked Life Data

3571631

Source:http://linkedlifedata.com/resource/pubmed/id/3571631

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-6-19
pubmed:abstractText
Results obtained from gel filtration showed that beta-lactoglobulin binds p-nitrophenyl phosphate with a stoichiometry of 1 mol of ligand per 18,360 monomer. Circular dichroic spectra confirmed the binding and implicated tryptophan and phenylalanine residues in the interaction. Fluorescence of the protein was quenched on binding also supporting complex formation; analysis of these data indicates that p-nitrophenyl phosphate binds to beta-lactoglobulin A with a dissociation constant of 31 microM. The B and C genetic variants of beta-lactoglobulin bind p-nitrophenyl phosphate with dissociation constants of 63 and 70 microM, respectively. In addition, a series of other nitrophenyl compounds and pyridoxal phosphate were also investigated by fluorescence analysis and found to bind to the protein. These results are discussed with respect to a recent hypothesis that beta-lactoglobulin binds retinol and is structurally related to serum retinol binding protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-0302
pubmed:author
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
252-8
pubmed:dateRevised
2001-3-23
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Binding of p-nitrophenyl phosphate and other aromatic compounds by beta-lactoglobulin.
pubmed:publicationType
Journal Article