Abstract
A variant antithrombin with reduced heparin affinity was shown by mass spectrometry sequencing and DNA amplification to have a substitution of a cysteine for an arginine at residue 24. The position of Arg-24 can be fixed within a 12 A radius from the bridge at Cys-21. This is compatible with findings in the homologous protease nexin-1 which indicate an extension of the binding site of heparin from the D-helix to under the adjacent amino-terminal pole.
Publication types
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Case Reports
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Research Support, Non-U.S. Gov't
MeSH terms
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Adult
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Antithrombin Proteins
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Antithrombins / genetics
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Antithrombins / metabolism*
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Base Sequence
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Binding Sites
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Carrier Proteins / genetics
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Carrier Proteins / metabolism
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Heparin / metabolism*
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Humans
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Male
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Molecular Sequence Data
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Oligonucleotide Probes
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Protein Conformation
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Structure-Activity Relationship
Substances
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Antithrombin Proteins
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Antithrombins
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Carrier Proteins
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Oligonucleotide Probes
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antithrombin Rouen IV
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Heparin