Abstract
Based on sequence information from tryptic peptides an almost full-size cDNA coding for the human vascular anticoagulant was isolated from a placental cDNA library and sequenced. The coding region was cloned into an Escherichia coli expression vector and the protein expressed at high levels. The recombinant protein was purified and found to be indistinguishable from its natural counterpart in several biological assays.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Annexins
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Base Sequence
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Blood Coagulation / drug effects*
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Calcium / metabolism
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Cloning, Molecular*
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DNA / analysis
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Electrophoresis, Polyacrylamide Gel
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Humans
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Molecular Sequence Data
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Peptides / genetics*
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Peptides / metabolism
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Peptides / pharmacology
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Phospholipids / metabolism
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Placenta / analysis
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RNA / analysis
Substances
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Annexins
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Peptides
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Phospholipids
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RNA
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DNA
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Calcium