K-252a, a potent inhibitor of protein kinase C from microbial origin.
- 1 January 1986
- journal article
- research article
- Published by Japan Antibiotics Research Association in The Journal of Antibiotics
- Vol. 39 (8) , 1059-1065
- https://doi.org/10.7164/antibiotics.39.1059
Abstract
K-252a, a metabolite isolated from the culture broth of Nocardiopsis sp. K-252a, was found to exhibit an extremely potent inhibitory activity on protein kinase C. The IC50 value was 32.9 nM.This publication has 14 references indexed in Scilit:
- Basic Protein in Brain Myelin Is Phosphorylated by Endogenous Phospholipid‐Sensitive Ca2+‐Dependent Protein KinaseJournal of Neurochemistry, 1982
- 2 TYPES OF CALCIUM-DEPENDENT PROTEIN PHOSPHORYLATIONS MODULATED BY CALMODULIN ANTAGONISTS - NAPHTHALENESULFONAMIDE DERIVATIVES1982
- Inhibition by phenothiazine antipsychotic drugs of calcium-dependent phosphorylation of cerebral cortex proteins regulated by phospholipid or calmodulinLife Sciences, 1981
- Phospholipid-sensitive calcium-dependent protein kinase: Inhibition by antipsychotic drugsBiochemical and Biophysical Research Communications, 1981
- Inhibitory action of chlorpromazine, dibucaine, and other phospholipid-interacting drugs on calcium-activated, phospholipid-dependent protein kinase.Journal of Biological Chemistry, 1980
- Calmodulin Plays a Pivotal Role in Cellular RegulationScience, 1980
- Calcium-dependent activation of a multifunctional protein kinase by membrane phospholipids.Journal of Biological Chemistry, 1979
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- [10] Assay of inorganic phosphate, total phosphate and phosphatasesPublished by Elsevier ,1966
- ADENOSINE 3',5'-PHOSPHATE IN BIOLOGICAL MATERIALS .1. PURIFICATION AND PROPERTIES OF CYCLIC 3',5'-NUCLEOTIDE PHOSPHODIESTERASE AND USE SF THIS ENZYME TO CHARACTERIZE ADENOSINE 3',5'-PHOSPHATE IN HUMAN URINE1962