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rdf:type |
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lifeskim:mentions |
umls-concept:C0015491,
umls-concept:C0018270,
umls-concept:C0035820,
umls-concept:C0221920,
umls-concept:C0225336,
umls-concept:C0598629,
umls-concept:C1167622,
umls-concept:C1514562,
umls-concept:C1552291,
umls-concept:C1552302,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
14
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|
pubmed:dateCreated |
1991-6-10
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pubmed:abstractText |
To determine the function and specificity in factor IX of the first epidermal growth factor (EGF)-like domain and the eight-amino acid hydrophobic stack encoded by exon C (residues 39-46), these domains were replaced by the corresponding polypeptide regions of factor X and chimeric proteins were produced in human embryo kidney cells. Both chimeras were activated by factor XIa at a rate similar to plasma factor IX and exhibited calcium-dependent fluorescence quenching similar to plasma factor IX. Both chimeras competed equally for binding to the endothelial cell receptor. Our findings make it unlikely that the first EGF-like domain or the hydrophobic stack of factor IX are responsible for the specific binding of factor IX to its endothelial cell receptor.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8797-800
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1851159-Amino Acid Sequence,
pubmed-meshheading:1851159-Animals,
pubmed-meshheading:1851159-Base Sequence,
pubmed-meshheading:1851159-Calcium,
pubmed-meshheading:1851159-Cattle,
pubmed-meshheading:1851159-Cell Line,
pubmed-meshheading:1851159-Cloning, Molecular,
pubmed-meshheading:1851159-DNA Mutational Analysis,
pubmed-meshheading:1851159-Endothelium, Vascular,
pubmed-meshheading:1851159-Epidermal Growth Factor,
pubmed-meshheading:1851159-Factor IX,
pubmed-meshheading:1851159-Factor X,
pubmed-meshheading:1851159-Humans,
pubmed-meshheading:1851159-Molecular Sequence Data,
pubmed-meshheading:1851159-Receptors, Cell Surface,
pubmed-meshheading:1851159-Recombinant Fusion Proteins,
pubmed-meshheading:1851159-Solubility,
pubmed-meshheading:1851159-Structure-Activity Relationship,
pubmed-meshheading:1851159-Transfection
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pubmed:year |
1991
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pubmed:articleTitle |
The role of the epidermal growth factor-1 and hydrophobic stack domains of human factor IX in binding to endothelial cells.
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pubmed:affiliation |
Department of Biology, University of North Carolina, Chapel Hill 27599.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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