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

Granules with broken membranes were isolated from sonicated, purified rat serosal mast cells on a Percoll gradient. When the granules were incubated with [gamma 32P]ATP and Mg2+ in the absence of exogenous protein kinases and substrates, one major radioactive band was recovered in the 44 K area after SDS/PAG electrophoresis. The phosphorylation reaction with ATP requires Mg2+ and 1 mM Mg2+ produces the maximal response. The initial reaction is rapid and the maximal response is seen at 30 degrees C. The reaction is enhanced by 0.05-0.5 microM cyclic AMP and is inhibited by Ca2+ (0.45 mM and higher). There is no obvious effect of phosphatidylserine and phorbol ester TPA on the reaction. The 44 K phosphorylated protein is made up of several components ranging in isoelectric point from approximately 7.6 to 6.6. This cyclic AMP-dependent phosphorylating activity in the granules may provide a mechanism by which the granules respond rapidly to cyclic AMP during mediator release.

Studies of phosphorylation in rat mast cells. Sixth report. Cyclic AMP-dependent protein phosphorylation in rat mast cell granule membranes.