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Updated: Sep 3, 2026

A Purification and In Vitro Activity Assay for a (p)ppGpp Synthetase from Clostridium difficile
Published on: November 3, 2018
3'-5' cAMP phosphodiesterase in pig liver nuclei
Abstract:
cAMP phosphodiesterase was partially purified from pig liver nuclei and some of its properties were investigated. The enzyme is a low km PDE. Inhibition by xanthine derivatives is in line with the behaviour of PDE from other mammalian sources, while small differences are observed towards nucleotides inhibitors. The enzyme is a chromatin-bound protein although no specific location related to transcriptional function could be demonstrated.
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