Abstract
Choline kinase has been partially purified from pea seedlings and its properties studied. Using sequence information from soya bean and other choline kinases, we have also isolated a cDNA encoding the enzyme. It encodes a protein of 343 amino acids (calculated molecular mass of 39785 Da), which shows 82% homology with the soya bean choline kinase. The protein has been expressed in Escherichia coli with very good activity and high expression levels.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Choline Kinase / genetics
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Choline Kinase / isolation & purification
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Choline Kinase / metabolism*
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Cloning, Molecular
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DNA, Complementary
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Escherichia coli
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Glycine max / enzymology
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Humans
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Male
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Mice
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Molecular Weight
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Pisum sativum / enzymology*
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Pisum sativum / genetics
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Rats
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Recombinant Proteins / metabolism
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Reverse Transcriptase Polymerase Chain Reaction
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Sequence Homology, Amino Acid
Substances
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DNA, Complementary
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Recombinant Proteins
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Choline Kinase