Pineal N-acetyltransferase is Inactivated by Disulfide-Containing Peptides: Insulin is the Most Potent

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-contain...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1981-07, Vol.213 (4507), p.571-573
Main Authors: Namboodiri, M. A. A., Favilla, J. T., Klein, D. C.
Format: Article
Language:English
Subjects:
Acetyltransferases - antagonists & inhibitors
Animals
Apoproteins
Axons
Citrates
Disulfides
Disulfides - pharmacology
Dithiothreitol - pharmacology
Enzymes
Ferritins
Hormones - pharmacology
Hydrogen-Ion Concentration
Insulin
Insulin - pharmacology
Kinetics
Male
Peptides - pharmacology
Pineal gland
Pineal Gland - enzymology
Polyribosomes
Rats
Sodium
Structure-Activity Relationship
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.7017937