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Crayfish abdominal muscle adenylate cyclase: Studies on the stimulation by a Ca²+-binding protein

D Sedlmeier, Gudrun Dieberg

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

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 languageEnglish
Pages (from-to)319-322
JournalBiochemical Journal
Volume211
Issue number2
Publication statusPublished - 1983

Keywords

  • Enzymes

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