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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)||Publication Date:||1983||Handle Link:||https://hdl.handle.net/1959.11/10523||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||Other Links:||http://www.biochemj.org/bj/211/bj2110319.htm||Statistics to Oct 2018:||Visitors: 221
|Appears in Collections:||Journal Article|
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