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 Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The particulate glucan synthetase preparation isolated from a homogenate of oat coleoptiles at 4 C lost 65% of its original activity after 1 day when the UDP-d-glucose substrate concentration was 5 x 10(-7)m to 1.0 x 10(-6)m. Storage of the particulate enzyme at -20 C or in liquid nitrogen did not prevent the enzyme from losing its activity. Incorporation of 0.5% hovine serum albumin into the medium stabilized the particulate enzyme at 0 C for 6 days and for at least 2 weeks in liquid nitrogen.When the particulate enzyme was treated with 8% digitonin, 40 to 50% of its activity appeared in the 100,000g supernatant fraction. The particulate and digitonin-solubilized enzyme preparations synthesized both beta-(1 --&gt; 4) and beta-(1 --&gt; 3) glucosyl linkages from UDP-d-glucose, but beta-(1 --&gt; 3) glucan was the main product at 1 x 10(-3)m UDP-d-glucose substrate. The activity of beta-(1 --&gt; 4) glucan synthetase was stimulated at least 10-fold in the presence of MgCl(2). A separation of beta-(1 --&gt; 4) and beta-(1 --&gt; 3) glucan synthetase activities could be achieved at 1 x 10(-3)m UDP-d-glucose when the digitonin-solubilized enzyme was adsorbed on a hydroxylapatite gel and then eluted with concentrated potassium phosphate buffer. The results indicate that the particulate enzyme contains two enzymes, one responsible for the synthesis of beta-(1 --&gt; 4) and another beta-(1 --&gt; 3) linkages in the glucan or glucans synthesized from UDP-d-glucose.

plant physiology

Solubilization and Separation of Uridine Diphospho-d-glucose: β-(1 → 4) Glucan and Uridine Diphospho-d-glucose:β-(1 → 3) Glucan Glucosyltransferases from Coleoptiles of <i>Avena sativa</i>

Solubilization and Separation of Uridine Diphospho-d-glucose: β-(1 → 4) Glucan and Uridine Diphospho-d-glucose:β-(1 → 3) Glucan Glucosyltransferases from Coleoptiles of Avena sativa