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 Plus annual

Presents the access of premium content as premium feature

Premium Content

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 Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

beta-Glucan synthases were solubilized by treating membrane preparations from suspension-cultured ryegrass (lolium multiflorum) endosperm cells with detergents. Of the seven detergents tested only digitonin and octyl glucoside dissociated active synthases from the membranes. The digitonin-solubilized enzymes produced 1,4-beta-glucans and 1,3:1,4-beta-glucans, whereas the digitonin-insoluble enzymes produced, in addition, 1,3-beta-glucans. Chromatography of the digitonin-solubilized beta-glucan synthases on DEAE-Sepharose resulted in their partial purification. The octyl glucoside-solubilized enzymes produced more 1,3-beta-glucans than did the membrane-bound preparations. These results suggest that the 1,3-beta-glucan synthase is a separate enzyme and is not involved in 1,3:1,4-beta-glucan synthesis. Digitonin not only dissociated synthases from the membranes, but also stimulated synthase activity. This effect may be related to the inhibition by digitonin of glucosyl transfer from UDP-glucose to form steryl glucosides.

Solubilization of β-glucan synthases from the membranes of cultured ryegrass endosperm cells