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Title: Crayfish abdominal muscle adenylate cyclase: Studies on the stimulation by a Ca²+-binding protein
Contributor(s): Sedlmeier, D (author); Dieberg, Gudrun  (author)orcid 
Publication Date: 1983
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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.
Publication Type: Journal Article
Source of Publication: Biochemical Journal, 211(2), p. 319-322
Publisher: Portland Press Ltd
Place of Publication: United Kingdom
ISSN: 0264-6021
Field of Research (FOR): 060107 Enzymes
Socio-Economic Outcome Codes: 970106 Expanding Knowledge in the Biological Sciences
Peer Reviewed: Yes
HERDC Category Description: C1 Refereed Article in a Scholarly Journal
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