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Science 31 July 1981:
Vol. 213. no. 4507, pp. 571 - 573
DOI: 10.1126/science.7017937
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Articles

Science, Vol 213, Issue 4507, 571-573
Copyright © 1981 by American Association for the Advancement of Science

articles

Pineal N-acetyltransferase is inactivated by disulfide-containing peptides: insulin is the most potent

MA Namboodiri, JT Favilla, and DC Klein

Pineal N-acetyltransferase can be inactivated in broken cell preparations by cystamine through a mechanism of thiol-disulfide exchange. Some, but not all, disulfide-containing peptides can inactivate this enzyme; the most potent inactivator is insulin. These findings suggest that a disulfide-containing peptide with high reactivity toward N-acetyltransferase may participate in the intracellular regulation of this enzyme.


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Pineal Serotonin N-Acetyltransferase: Expression Cloning and Molecular Analysis.
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