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Regulation of spermidine acetyltransferase activity by phosphorylation and dephosphorylation.

Authors
  • Grillo, M A
Type
Published Article
Journal
The Italian journal of biochemistry
Publication Date
Jan 01, 1983
Volume
32
Issue
3
Pages
167–173
Identifiers
PMID: 6654645
Source
Medline
License
Unknown

Abstract

Spermidine acetyltransferase activity is more than 10-fold higher in the pancreas of a 20-hr-fasted than in that of a fed chicken. The preparation of the fed bird inactivates the other. The effect is due to a thermolabile component of microsomes, and is also obtained with alkaline phosphatase. The inactivated preparation partially recovers its activity through phosphorylation catalyzed by a cAMP-dependent protein kinase. The results presented strongly suggest that spermidine acetyltransferase activity is regulated by phosphorylation and dephosphorylation.

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