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Related Experiment Videos

Rabbit liver acetyl-CoA synthetase.

G Woodnutt, D S Parker

    The Biochemical Journal
    |November 1, 1978
    PubMed
    Summary
    This summary is machine-generated.

    Acetyl-CoA synthetase activity was primarily found in the cytosol of rabbit liver cells. Adding butyrate or propionate did not affect this enzyme activity.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Enzymology

    Background:

    • Acetyl-CoA synthetase (EC 6.2.1.1) plays a crucial role in cellular metabolism by activating fatty acids.
    • Understanding the subcellular localization and regulation of this enzyme is vital for metabolic research.

    Purpose of the Study:

    • To determine the precise subcellular localization of Acetyl-CoA synthetase activity in rabbit liver.
    • To investigate the effect of short-chain fatty acids (butyrate and propionate) on Acetyl-CoA synthetase activity.

    Main Methods:

    • Rabbit liver homogenates were fractionated to isolate different cellular components.
    • Acetyl-CoA synthetase activity was assayed in these subcellular fractions.
    • Enzyme activity was measured in the presence and absence of butyrate and propionate.

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    Main Results:

    • Acetyl-CoA synthetase activity was predominantly detected in the cytosolic fraction of rabbit liver.
    • No significant inhibition or alteration of enzyme activity was observed upon the addition of 5-20 mM butyrate or propionate.

    Conclusions:

    • The primary location of Acetyl-CoA synthetase in rabbit liver is the cytosol.
    • Short-chain fatty acids like butyrate and propionate do not appear to modulate the activity of cytosolic Acetyl-CoA synthetase in this model system.