Pea choline kinase: purification, properties and isolation of a cDNA

Biochem Soc Trans. 2000 Dec;28(6):721-3.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Choline Kinase / genetics
  • Choline Kinase / isolation & purification
  • Choline Kinase / metabolism*
  • Cloning, Molecular
  • DNA, Complementary
  • Escherichia coli
  • Glycine max / enzymology
  • Humans
  • Male
  • Mice
  • Molecular Weight
  • Pisum sativum / enzymology*
  • Pisum sativum / genetics
  • Rats
  • Recombinant Proteins / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Homology, Amino Acid

Substances

  • DNA, Complementary
  • Recombinant Proteins
  • Choline Kinase