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

Authors :
John L. Harwood
Abdulrahman L. Al-Malki
Andrew P. Morby
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