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

Al-Malki, A., Morby, Andrew P. and Harwood, John L. 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: Biosciences
Publisher: Portland Press
ISSN: 0300-5127
Last Modified: 04 Jun 2017 06:37
URI: http://orca.cf.ac.uk/id/eprint/62883

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