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May 1, 1996Journal of Biological ChemistryOpen Access

Suppression of Creatine Kinase-catalyzed Phosphotransfer Results in Increased Phosphoryl Transfer by Adenylate Kinase in Intact Skeletal Muscle

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Population

Intact diaphragm muscle from rats

Comparison

Graded inhibition of creatine kinase activity by… vs Noncontracting muscle from untreated rats

Design

Preclinical

Authors

PDPetras P. DzejaRZRobert J. ZeleznikarNGNelson D. Goldberg

Discussion

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Overview

AK may compensate for CK loss to preserve ATP flux in muscle; leaves open relevance to human cardiac energetics.

Structured PICO

P
Population
Intact diaphragm muscle from rats
I
Intervention
Graded inhibition of creatine kinase (CK) activity by 2,4-dinitrofluorobenzene
C
Comparator
Noncontracting muscle from untreated rats
O
Outcome
Kinetics of creatine kinase (CK) and adenylate kinase (AK) activities monitored by 18O phosphoryl oxygen exchangesurrogate

Creatine kinase and adenylate kinase operate as interrelated cellular high energy phosphoryl transfer systems in intact muscle.

Cite This Study

Dzeja et al. (1996) studied this question.

synapsesocial.com/papers/6a855d7367f5f0039bad93e5https://doi.org/10.1074/jbc.271.22.12847
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Evidence for compartmentalized adenylate kinase catalysis serving a high energy phosphoryl transfer function in rat skeletal muscle.1990 · 92 citations
  2. 2Kinetics and compartmentation of energy metabolism in intact skeletal muscle determined from 18O labeling of metabolite phosphoryls1991 · 44 citations
  3. 3Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the ‘phosphocreatine circuit’ for cellular energy homeostasis1992 · 2,032 citations
  4. 4THE CREATINE-CREATINE PHOSPHATE ENERGY SHUTTLE1985 · 760 citations