Stimulation of proteolysis on calmodulin
| Autor: | Wu-Nan Kuo, A. Robinson, M. N. Jean, U. Ganesan, A.K. Mack, S. Sen |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Electrophoresis
Proteases Calmodulin Proteolysis medicine.medical_treatment General Biochemistry Genetics and Molecular Biology Endopeptidases medicine Animals General Pharmacology Toxicology and Pharmaceutics Gel electrophoresis Protease L-Lactate Dehydrogenase medicine.diagnostic_test biology Binding protein S100 Proteins Caseins Deoxyguanine Nucleotides RNA General Medicine Molecular biology Parvalbumins Biochemistry DNA Viral biology.protein RNA Viral Cattle Peptides Parvalbumin |
| Zdroj: | Life Sciences. 47:291-297 |
| ISSN: | 0024-3205 |
| DOI: | 10.1016/0024-3205(90)90586-g |
| Popis: | The proteolysis of calmodulin by fungal protease (type XIX) was greatly enhanced in the presence of dGTP and MS2 RNA. Whereas, only moderate proteolytic activation on bacterial proteases (type XXVI) was observed in the presence of MS2 RNA. No appreciable proteolysis of calmodulin by bacterial protease (type IX) was observed. Proteolytic fragments of calmodulin cleaved by fungal protease exhibited unusual low mobility during SDS-polyacrylamide gel electrophoresis. Similar decreased electrophoretic mobility was also noted in the proteolytic fragments of other Ca2+-binding proteins including S-100A protein and parvalbumin. |
| Databáze: | OpenAIRE |
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