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Related Experiment Videos

Hepatic microsomal Ca2+-dependent ATPase. Calmodulin-dependence and partial purification.

P B Moore, N Kraus-Friedmann

    The Biochemical Journal
    |July 15, 1983
    PubMed
    Summary

    Hepatic microsomal fractions contain bound calmodulin, a protein that regulates calcium uptake and ATPase activity. This study demonstrates calmodulin

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    Area of Science:

    • Biochemistry
    • Cell Biology

    Background:

    • Hepatic microsomal fractions are crucial for cellular processes.
    • Calmodulin is a key calcium-binding protein involved in cellular signaling.

    Purpose of the Study:

    • To investigate the role of tightly bound calmodulin in hepatic microsomal fractions.
    • To characterize the calmodulin-dependent calcium uptake and ATPase activity.

    Main Methods:

    • Affinity chromatography was used to isolate bound calmodulin.
    • EGTA treatment was employed to partially remove calmodulin.
    • Calcium-45 uptake assays and Ca2+-dependent ATPase activity measurements were performed.
    • Trifluoperazine (TFP) inhibition and calmodulin antibodies were used for validation.

    Main Results:

    • Tightly bound calmodulin was identified in hepatic microsomes.
    • Partial calmodulin removal stimulated 45Ca2+ uptake, which was reversed by adding calmodulin or inhibited by TFP.
    • A Ca2+-dependent ATPase was partially purified, showing a 500-fold increase in specific activity with added calmodulin.
    • Calmodulin antibodies blocked the stimulatory effect, confirming calmodulin's role.

    Conclusions:

    • Hepatic microsomal fractions contain tightly bound calmodulin that regulates Ca2+ uptake and ATPase activity.
    • The findings suggest other calmodulin-sensitive processes may exist in hepatic microsomes.

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