Linked Life Data

893396

Source:http://linkedlifedata.com/resource/pubmed/id/893396

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1977-10-20
pubmed:abstractText
Affinity labeling of human serum prealbumin with N-bromoacetyl-L-thyroxine (BrAcT4) was used to investigate the binding domain for L-thyroxine (T4) on prealbumin. Fluorescence titration with 8-anilinonaphthalene-1-sulfonate revealed a strong and a weak binding site for BrAcT4 (K1 = 1 X 10(8) M-1; K2 = 1 X 10(6) M-1). The reaction of BrAcT4 with prealbumin to form a covalent bond was inhibited in the presence of T4 and binding of T4 to prealbumin was nearly abolished after affinity labeling with BrAcT4. Affinity labeling with 2 mol of BrAcT4/mol of prealbumin resulted in covalent binding of 1 mol of ligand. Acid hydrolysis of affinity-labeled prealbumin gave Nepsilon-carboxymethyllysine and iminodiacetic acid, the latter being derived from the NH2-terminal glycine. A combination of analytical procedures, including tryptic digestion after maleylation, cyanogen bromide cleavage, digestion with yeast protease C, and sequential Edman degradations, revealed that the Nepsilon-carboxymethyllysine was derived from lysine-9 and lysine-15 and that the affinity label had distributed itself among glycine-1, lysine-9, and lysine-15 in a ratio of 29:63:8.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
252
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6076-81
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Affinity labeling of human serum prealbumin with N-bromoacetyl-L-thyroxine.
pubmed:publicationType
Journal Article