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

Two forms of a cAMP phosphodiesterase were found in the superior cervical ganglia of the rat. The influence of various detergents on solubility and activity of the enzyme was studied. Two Km values were determined, one of 0.9mum and the other 270mum cAMP. Separation by polyacrylamide disc electrophoresis revealed four distinct peaks of enzyme activity. One of these activities was increased when ganglia were incubated with adrenaline for at least 4 h. The increase caused by adrenaline was unaffected when ganglia were pre-incubated with cycloheximide, but was blocked in the presence of propranolol, a beta-adrenergic antagonist. Incubation with dibutyryl cAMP for 4 h mimicked the effect of adrenaline. Brief incubation with adrenaline was without effect. Electrophoresis in the presence of 0.1% Lubrol W, a non-ionic detergent, showed that one band of activity disappeared, while the main peak of enzyme activity increased in size. Two-dimensional starch gel electrophoresis confirmed the results of the disc electrophoresis.

hoppe-seyler's zeitschrift für physiologische chemie

3′:5′-Nucleotide Phosphodiesterase in the Superior Cervical Ganglion of the Rat. Evidence for Multiple Forms and Influence of the β-Adrenergic Receptor System in the Electrophoretic Pattern of the Enzyme