Studies on the Degradation of Tyrosine Aminotransferase in Hepatoma Cells in Culture: INFLUENCE OF THE COMPOSITION OF THE MEDIUM AND ADENOSINE TRIPHOSPHATE DEPENDENCE

Avram Hershko; Gordon M. Tomkins

doi:10.1016/S0021-9258(18)62470-6

CHEMISTRY AND METABOLISM OF MACROMOLECULES| Volume 246, ISSUE 3, P710-714, February 10, 1971

Studies on the Degradation of Tyrosine Aminotransferase in Hepatoma Cells in Culture

INFLUENCE OF THE COMPOSITION OF THE MEDIUM AND ADENOSINE TRIPHOSPHATE DEPENDENCE

Avram Hershko
Avram Hershko
Affiliations
From the Department of Biochemistry and Biophysics, University of California, San Francisco, San Fran California 94122
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Gordon M. Tomkins
Gordon M. Tomkins
Affiliations
From the Department of Biochemistry and Biophysics, University of California, San Francisco, San Fran California 94122
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Open AccessPublished:February 10, 1971DOI:https://doi.org/10.1016/S0021-9258(18)62470-6

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The degradation of glucocorticoid-induced tyrosine amino-transferase and of general cellular proteins in hepatoma (HTC) cells in culture is enhanced by the deprivation of both amino acids and of serum, and by lowering the pH of the medium. This "enhanced" degradation, but not the normal degradation, is inhibited by inhibitors of protein synthesis.

Sodium fluoride and other inhibitors of cellular ATP production profoundly inhibit the degradation of tyrosine aminotransferase and other proteins. This effect was shown, in the case of tyrosine aminotransferase, to be rapidly reversible and exerted by a mechanism different from the inhibition of protein synthesis. It is proposed that ATP participates in an early phase of enzyme degradation.

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Published online: February 10, 1971

Received: September 3, 1970

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DOI: https://doi.org/10.1016/S0021-9258(18)62470-6

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