Chapter title |
Assay of NAT Activity
|
---|---|
Chapter number | 12 |
Book title |
Endocannabinoid Signaling
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3539-0_12 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3537-6, 978-1-4939-3539-0
|
Authors |
Toru Uyama, Natsuo Ueda |
Editors |
Mauro Maccarrone |
Abstract |
In animal tissues, N-acyltransferase (NAT) catalyzes the first reaction in the biosynthetic pathway of bioactive N-acylethanolamines, in which an acyl chain is transferred from the sn-1 position of the donor phospholipid, such as phosphatidylcholine, to the amino group of phosphatidylethanolamine, resulting in the formation of N-acylphosphatidylethanolamine. NAT has long been known to be stimulated by Ca(2+), and hence it has been referred to as Ca(2+)-dependent NAT. On the other hand, members of the phospholipase A/acyltransferase (PLA/AT) family (also known as HRAS-like suppressor family) show Ca(2+)-independent NAT activity. In this chapter, we describe (1) partial purification of Ca(2+)-dependent NAT from rat brain, (2) purification of recombinant PLA/AT-2, and (3) NAT assay using radiolabeled substrate. |
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