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The substructure of phosphodiesterase as established by radiation inactivation
Author(s) -
Ottolenghi P.,
Ellory J.C.,
Klein R.A.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80758-8
Subject(s) - phosphodiesterase , calmodulin , chemistry , substructure , biophysics , radiation , biochemistry , monomer , enzyme , biology , physics , optics , organic chemistry , structural engineering , engineering , polymer
A model for the activation of phosphodiesterase by calmoduling based on a conversion of inactive dimers to active monomers, derived from radiation inactivation studies J. Biol. Chem. (1981) 256, 11351–11355 has been re‐examined using a simple probability argument. We conclude that the original model is not supported by the radiation inactivation studies, since our analysis of this model would predict that the rate of radiation inactivation of calmodulin‐dependent phosphodiesterase activity be exactly twice that for the decay in total activity in marked contrast with the results obtained.