Heat-resistant inhibitors of protein kinase C from bovine brain
| Autor: | I, Pribilla, H, Krüger, K, Buchner, H, Otto, W, Schiebler, D, Tripier, F, Hucho |
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| Rok vydání: | 1988 |
| Předmět: |
Proteases
Calmodulin Proteolysis Molecular Sequence Data Nerve Tissue Proteins Biochemistry Cytosol medicine Animals Trypsin Amino Acid Sequence Protein kinase A Protein Kinase C Protein kinase C biology medicine.diagnostic_test Kinase Brain Enzyme Activation Molecular Weight Kinetics Enzyme inhibitor biology.protein Cattle |
| Zdroj: | European Journal of Biochemistry. 177:657-664 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1988.tb14420.x |
| Popis: | Bovine brain cytosol is shown to contain two heat-resistant inhibitors of protein kinase C, with the following characteristics: 1. One protein kinase C inhibitor can be easily purified to homogeneity. Evidence is presented that this polypeptide of Mr 19,000 is calmodulin. It inhibits protein kinase C with an EC50 of about 2.5 microM and the inhibition is Ca2+-independent. It inhibits only intact protein kinase C. Removal of the regulatory domain of protein kinase C, by limited proteolysis with trypsin, abolishes the inhibition. 2. Another protein kinase C inhibitory activity has been partially purified. Its Mr is low (Mr 600-700, as estimated by gel chromatography). It is not digested by proteases, is hydrophilic, acid- and alkali-resistant, acts Ca2+-independently, and, in contrast to calmodulin, inhibits even the catalytic fragment of protein kinase C after removal of the regulatory domain by limited proteolysis. This inhibition is, at least partially, due to a competition with ATP. Besides protein kinase C, calcium/calmodulin-dependent protein kinase II is inhibited to a similar extent. cAMP-dependent protein kinase is not affected. |
| Databáze: | OpenAIRE |
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