Abstract
A Ca2+, calmodulin-dependent protein kinase from rat brain with a MW of 640,000 phosphorylated calmodulin-sensitive phosphodiesterase from the brain cytosol. The Km of the enzyme for the phosphodiesterase was 5.0 μM and the Vmax was 212 nmol/mg/min. The amount of phosphate incorporated into the phosphodiesterase was 0.7 mol/mol subunit. Phosphorylation of the phosphodiesterase enhanced the enzyme activity by about 20% for hydrolysis of a higher concentration of cyclic AMP.
| Original language | English |
|---|---|
| Pages (from-to) | 493-499 |
| Number of pages | 7 |
| Journal | Life Sciences |
| Volume | 35 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 1984 Jul 30 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Pharmacology, Toxicology and Pharmaceutics(all)
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Fukunaga, K., Yamamoto, H., Tanaka, E., Iwasa, T., & Miyamoto, E. (1984). Phosphorylation and activation of calmodulin-sensitive cyclic nucleotide phosphodiesterase by a brain Ca2+, calmodulin-dependent protein kinase. Life Sciences, 35(5), 493-499. https://doi.org/10.1016/0024-3205(84)90242-X