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Pea choline kinase: purification, properties and isolation of a cDNA
- Source :
- Biochemical Society Transactions. 28:721-723
- Publication Year :
- 2000
- Publisher :
- Portland Press Ltd., 2000.
-
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 Eschericiha coli with very good activity and high expression levels.
Details
- ISSN :
- 14708752 and 03005127
- Volume :
- 28
- Database :
- OpenAIRE
- Journal :
- Biochemical Society Transactions
- Accession number :
- edsair.doi...........b11e4e798e2d73e7167ef7a918882f86
- Full Text :
- https://doi.org/10.1042/bst0280721