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. 1966 Feb;41(2):313–318. doi: 10.1104/pp.41.2.313

Effect of Cycocel Derivatives and Gibberellin on Choline Kinase and Choline Metabolism 1

Kiichiro Tanaka 1,2, N E Tolbert 1
PMCID: PMC1086338  PMID: 5908635

Abstract

Cycocel stimulated the activity of partial purified choline kinase from spinach or squash leaves, but it inhibited the activity of yeast choline kinase. The activity of different Cycocel analogs on plant growth corresponded to their stimulatory effect on the isolated choline kinase. Cycocel had no effect upon the activity of a plant phosphatase which hydrolyzed phosphorylcholine nor upon adenosine triphosphatase from wheat roots or leaves.

Gibberellin A3 inhibited choline kinase activity and reversed the stimulatory effect of Cycocel on the kinase.

Total choline kinase activity per squash plant was not greatly increased by Cycocel treatment. However, on the basis of fresh weight, total kinase activity was increased by Cycocel treatment. Gibberellin A3 partially reversed these increases. Treatment with Cycocel plus indoleacetic acid resulted in a large increase in choline kinase activity.

The same distribution of tracer among phosphorylcholine, choline and betaine was observed when either phosphorylcholine-C14 or choline-C14 was fed to barley or wheat roots. Cycocel stimulated the incorporation of choline-C14 into the insoluble fraction and into lipids. Cycocel inhibited phosphorylcholine uptake by roots.

Thus Cycocel stimulated choline kinase activity and the utilization of choline-C14. The effect of Cycocel upon kinase activity in vivo and in vitro was reversed by gibberellin A3.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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