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The conversion of ATP to IMP by muscle surface enzymes
Author(s) -
Dunkley C. R.,
Manery J. F.,
Dryden E. E.
Publication year - 1966
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1040680305
Subject(s) - adenylate kinase , amp deaminase , inosine monophosphate , adenosine monophosphate , enzyme , atpase , chemistry , inosine , nucleotide , biochemistry , tris , adenosine deaminase , ouabain , adenosine , adenosine triphosphate , incubation , ammonia , cyclase , adenine nucleotide , phosphate , sodium , organic chemistry , gene
These experiments showed that an isolated muscle bundle could be used to study, simultaneously, ion transport and the activity of surface enzymes. Frog muscles were carefully dissected and incubated for four hours in Ringer's solution containing a tris buffer and 3 mM ATP; at various times samples of the medium were chromatographed and analysed spectrophotometrically for nucleotide content. Samples of the final medium were analysed for inorganic phoshpate and for ammonia. The results demonstrated the conversion of adenosine triphosphate to inosine monophosphate, via adenosine diphosphate and adenosine monophosphate. Under the conditions of the experiment IMP was detected on chromatograms within 20 minutes of incubation; at the end of four hours the media had concentrations of 2.3 mM IMP, 4.4 mM inorganic phosphate and 2.6 mM ammonia, showing a stoichiometric relation among the products formed. There was convincing evidence that the enzymes involved (ATPase, adenylate kinase and AMP deaminase) must be situated close to or on the muscle surface. No effect of ouabain (1 μM) on the activity of the ATPase, adenylate kinase or deaminase could be found in these experiments, but the drug inhibited Na and K recovery from a Na‐loaded, K‐depleted state.