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Related Experiment Videos

Creatine kinase.

R Bais, J B Edwards

    Critical Reviews in Clinical Laboratory Sciences
    |June 1, 1982
    PubMed
    Summary
    This summary is machine-generated.

    Creatine kinase (CK) is crucial in muscle energy. Understanding its properties and isoenzymes aids in diagnosing conditions like heart attacks and muscle injuries by analyzing CK levels in biological fluids.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Clinical Chemistry

    Background:

    • Creatine kinase (CK) is abundant in skeletal and cardiac muscle, with lower levels in the brain and GI tract.
    • CK exists as three isoenzymes, each with two subunits and critical cysteine residues.
    • CK properties influence its stability, assay conditions, and isoenzyme identification.

    Purpose of the Study:

    • To review the properties of creatine kinase.
    • To explore the relationship between CK properties and its determination in biological fluids.
    • To discuss factors influencing total and isoenzyme CK activities for accurate clinical interpretation.

    Main Methods:

    • Purification of creatine kinase from various tissues.
    • Analysis of kinetic and physical properties of the enzyme.

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  • Examination of factors affecting creatine kinase activity in biological samples.

    • Main Results:

    • Creatine kinase consists of two subunits and exists as three isoenzymes.
    • Essential cysteine residues are present in creatine kinase.
    • Creatine kinase activity in serum increases rapidly during myocardial infarction and skeletal muscle trauma.

    Conclusions:

    • Understanding creatine kinase properties is vital for accurate assays and isoenzyme identification.
    • Knowledge of factors influencing CK activity is essential for interpreting elevated levels in clinical diagnostics.
    • This review emphasizes the link between enzyme characteristics and clinical applications of creatine kinase measurements.