English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

The gibberellin (GA) binding properties of a cytosol fraction from hypocotyls of cucumber (Cucumis sativus L. cv National Pickling) were examined using a DEAE filter paper assay, [(3)H]GA(4), and over 20 GAs, GA derivatives and other growth regulators. The results demonstrate structural specificity of the binding protein for gamma-lactonic C-19 GAs with a 3 beta-hydroxyl and a C-6 carboxyl group. Additional hydroxylations of the A, C, or D ring of the ent-gibberellane skeleton and methylation of the C-6 carboxyl impede or abolish binding affinity. Bioassay data are generally supported by the in vitro results but significantly GA(9) and GA(36), both considered to be precursors of GA(4) in cucumber, show no affinity for the binding protein. The results are discussed in relation to the active site of the putative GA(4) receptor in cucumber.

Competition for in Vitro [3H]Gibberellin A4 Binding in Cucumber by Gibberellins and Their Derivatives

Competition for in Vitro [³H]Gibberellin A₄ Binding in Cucumber by Gibberellins and Their Derivatives