Creatine kinase (CK) is an enzyme that catalyzes the reversible phosphorylation of creatine (Cr) by adenosine triphosphate (ATP). Physiologically, when muscle contracts, ATP is converted to adenosine diphosphate (ADP), and CK catalyzes the rephosphorylation of ADP to ATP using creatine phosphate as the phosphorylation reservoir. The CK enzyme is a dimer composed of subunits derived from either muscle (M) or brain (B). Three isoenzymes have been identified: striated muscle (MM), heart tissue (MB), and brain (BB). Normal serum CK is predominantly the CK-MM isoenzyme. Serum CK concentrations are reflective of muscle mass causing males to have higher concentrations than females. CK may be measured to evaluate myopathy and to monitor patients with rhabdomyolysis for acute kidney injury.
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