title: Pea choline kinase: purification, properties and isolation of a cDNA.
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.
authors.affiliation: School of Biosciences, Cardiff University, P.O. Box 911, Cardiff CF10 3US, Wales, UK.
authors.forename: A
authors.initials: A
authors.lastname: Al-Malki
authors.forename: A
authors.initials: A
authors.lastname: Morby
authors.forename: J L
authors.initials: JL
authors.lastname: Harwood
mesh_terms: D000818:Animals; D002797:Choline Kinase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004926:Escherichia coli; D006801:Humans; D008297:Male; D051379:Mice; D008970:Molecular Weight; D018532:Pisum sativum / Q000201:enzymology* / Q000235:genetics; D051381:Rats; D011994:Recombinant Proteins / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid; D013025:Glycine max / Q000201:enzymology
chemical_list: D018076:DNA, Complementary; D011994:Recombinant Proteins; D002797:Choline Kinase