Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 571-573 |
| Number of pages | 3 |
| Journal | Science |
| Volume | 213 |
| Issue number | 4507 |
| DOIs | |
| State | Published - 1981 |
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