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Human renal carbonic anhydrase. Purification and properties

J Wistrand, S Lindahl, T Wåhlstrand

    European Journal of Biochemistry
    |September 1, 1975
    PubMed
    Summary

    Human kidney carbonic anhydrase, isolated using affinity chromatography, is biochemically and kinetically similar to carbonic anhydrase C found in red blood cells. This suggests the kidney enzyme is likely identical to this high-activity erythrocyte form.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Human Physiology

    Background:

    • Carbonic anhydrase is a crucial enzyme in physiological processes.
    • Understanding tissue-specific forms of carbonic anhydrase is important for human health.
    • Previous research has identified various carbonic anhydrase isoenzymes in humans.

    Purpose of the Study:

    • To isolate and characterize carbonic anhydrase from human kidney tissue.
    • To compare the properties of the renal carbonic anhydrase with known human isoenzymes.
    • To determine if the kidney enzyme is identical to the erythrocyte form, carbonic anhydrase C.

    Main Methods:

    • Isolation of carbonic anhydrase from blood-free human donor kidneys.
    • Purification using biospecific affinity chromatography on a sulfanilamide-agarose column.

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  • Characterization through ultracentrifugation, electrophoresis, isoelectric focusing, immunodiffusion, amino acid composition analysis, and kinetic studies (stopped-flow pH-indicator technique).

    • Main Results:

    • A single, homogenous soluble form of carbonic anhydrase was isolated from the human kidney.
    • The renal enzyme exhibited identical amino acid composition, chromatographic, electrophoretic, and immunochemical properties to human carbonic anhydrase C.
    • Kinetic analysis revealed similar behavior between the renal enzyme and human carbonic anhydrase C.

    Conclusions:

    • The cytoplasmic carbonic anhydrase of the human kidney is highly similar, potentially identical, to human carbonic anhydrase C.
    • This finding has implications for understanding carbonic anhydrase function in renal physiology.
    • The study confirms the presence of carbonic anhydrase C in human kidney tissue.