Abstract
A plasma-membrane preparation of crayfish muscle showed an adenylate cyclase activity which is inhibited to about 80% of its original activity by 100 μM-EGTA. Measurements of the enzyme activity in the presence of 100 μM-EGTA and various concentrations of Ca²+ revealed an increase in enzyme activity of about 400%, indicating an adenylate cyclase which is dependent on Ca²+ for activity. Fluphenazine (1 mM), a blocker of the Ca²+-binding protein calmodulin, decreased enzyme activity to zero. The enzyme can be re-activated by the addition of certain concentrations of calmodulin to the assay medium. This suggests that crayfish muscle adenylate cyclase is dependent on Ca²+ and calmodulin for activity.
| Original language | English |
|---|---|
| Pages (from-to) | 319-322 |
| Journal | Biochemical Journal |
| Volume | 211 |
| Issue number | 2 |
| Publication status | Published - 1983 |
Keywords
- Enzymes
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