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

Al-Malki, A., Morby, Andrew P. and Harwood, John L. ORCID: https://orcid.org/0000-0003-2377-2612 2000. Pea choline kinase: purification, properties and isolation of a cDNA. Biochemical Society Transactions 28 (6) , pp. 721-723. 10.1042/0300-5127:0280721

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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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Biosciences
Publisher:	Portland Press
ISSN:	0300-5127
Last Modified:	27 Oct 2022 08:37
URI:	https://orca.cardiff.ac.uk/id/eprint/62883

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