Abstract
A chemically synthesized polynucleotide sequence coding for bovine liver low molecular weight acid phosphatase (which possesses phosphotyrosine-protein phosphatase activity) has been cloned in a E. coli expression vector. The recombinant protein retains correct affinity for substrate and inhibitors but shows a reduced specific activity.
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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Animals
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Base Sequence
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Cattle
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Cloning, Molecular
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Escherichia coli / metabolism*
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Gene Expression
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Genes, Synthetic*
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Kinetics
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Liver / enzymology
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Molecular Sequence Data
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Phosphoprotein Phosphatases / biosynthesis
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Phosphoprotein Phosphatases / chemistry
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Phosphoprotein Phosphatases / genetics*
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Phosphoprotein Phosphatases / metabolism
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Protein Tyrosine Phosphatases
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Substrate Specificity
Substances
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Recombinant Proteins
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Phosphoprotein Phosphatases
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Protein Tyrosine Phosphatases