The direct measurement of protein kinase C (PKC) activity in isolated membranes using a selective peptide substrate
| Autor: | Jon P. Durkin, Balu Chakravarthy, Ross E. Williams, Alexandra Bussey, Marianna Sikorska, James F. Whitfield |
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| Rok vydání: | 1991 |
| Předmět: |
Lymphoma
Molecular Sequence Data Biophysics Peptide Biochemistry Cell Line Substrate Specificity chemistry.chemical_compound Methods Tumor Cells Cultured Amino Acid Sequence Phosphorylation Molecular Biology Protein kinase C Protein Kinase C chemistry.chemical_classification Kinase Cell Membrane Cell Biology Phosphatidylserine Kinetics Membrane Enzyme chemistry Cell culture Tetradecanoylphorbol Acetate Calcium Peptides |
| Zdroj: | Analytical biochemistry. 196(1) |
| ISSN: | 0003-2697 |
| Popis: | A protein kinase C (PKC)-selective peptide substrate was used to develop a method for measuring PKC activity directly and quantitatively in isolated cell membranes without prior detergent extraction and reconstitution of the enzyme with phosphatidylserine and TPA in the presence of excess Ca2+. This simple and rapid method can reliably measure changes in membrane-associated PKC activity induced by various bioactive compounds such as hormones and growth factors. Also, this method, which measures PKC activity in its native membrane-associated state, has the advantage of being able to distinguish between active and inactive PKC associated with cell membranes. |
| Databáze: | OpenAIRE |
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