Linked Life Data

91613

Source:http://linkedlifedata.com/resource/pubmed/id/91613

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1980-1-28
pubmed:abstractText
The binding of bilirubin and the polyene fatty acids cis-parinaric acid and cis-eleostearic acid to human alpha-fetoprotein was studied using fluorescence quenching and fluorescence enhancement techniques. alpha-Fetoprotein has three fatty acid binding sites of decreasing affinity (association constants 2.1 x 10(7) M-1 9.1 X 10(5) M-1, and 1.4 x 10(5) M-1) and one relatively strong and one relatively weak bilirubin binding site (association constants 1.1 x 10(7) M-1 and 1.8 x 10(5) M-1). These association constants are slightly weaker than the corresponding association constants for binding to human albumin. Competition experiments failed to show preferential binding of polyunsaturated fatty acids. Fluorescence quenching was used to determine 11 ligand-ligand and ligand-tryptophanyl residue distances. Each of these 11 calculated distances (ranging from 19 A to 32 A) was within 5 A of the corresponding distances measured previously for human albumin (Berde, C.B., Hudson, B.S., Simoni, R.D., and Sklar, L.A. 1979, J. Biol. Chem. 254, 391-400). Thus, in addition to previously described sequence homology, immunologic cross-reactivity, and other similarities, human albumin and human alpha-fetoprotein have functional and geometric homologies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
254
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12609-14
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Human alpha-fetoprotein. Fluorescence studies on binding and proximity relationships for fatty acids and bilirubin.
pubmed:publicationType
Journal Article