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Pea choline kinase: purification, properties and isolation of a cDNA
Journal article   Peer reviewed

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

A Al-Malki, A Morby and J L Harwood
Biochemical Society transactions, Vol.28(6), pp.721-723
01/12/2000
PMID: 11171184

Abstract

Biochemistry & Molecular Biology Life Sciences & Biomedicine Science & Technology
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.

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