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Activation of Membrane-Bound Adenylate Cyclase by Glucagon in Neurospora crassa
Author(s) -
Mirtha M. Flawiá,
Héctor N. Torres
Publication year - 1972
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.69.10.2870
Subject(s) - glucagon , glycogen phosphorylase , neurospora crassa , adenylate kinase , glycogenolysis , cyclase , glycogen , neurospora , biology , biochemistry , incubation , medicine , enzyme , endocrinology , chemistry , hormone , mutant , gene
Membrane-bound adenylate cyclase in Neurospora crassa is activated by glucagon. Half-maximal effect is observed at hormone concentrations of about 10 nM. After solubilization of the enzyme with Lubrol-PX, the glucagon effect is lost. Incubation of neurospora cells with glucagon leads to a decrease in the activity of glycogen synthetase (EC 2.4.1.11) and to an increase in the activity of glycogen phosphorylase (EC 2.4.1.1) and in the rate of glycogenolysis.

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