Abstract
This study demonstrates the metabolic transformation of prostaglandin A1 (PGA1) by guinea pig and rat liver microsomes. The transformation, which required NADPH and oxygen, yielded polar (presumably hydroxylated) products. Incubations with guinea pig liver microsomes yielded one zone of product on tlc, whereas rat liver microsomes produced two discernable metabolic zones. It was demonstrated that PGA1 metabolism in the guinea pig and the rat was inhibited by the addition of SKF-525A, metyrapone, carbon monoxide and cytochrome C; nicotinamide (10 mM) inhibited only the guinea pig system. These findings indicate that the enzymatic activity responsible for PGA1 metabolism is composed of a typical cytochrome P-450 monooxygenase system.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 507-513 |
| Number of pages | 7 |
| Journal | Life Sciences |
| Volume | 18 |
| Issue number | 5 |
| DOIs | |
| State | Published - Mar 1 1976 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Pharmacology
Cite this
Metabolism of prostaglandin A1 by hepatic microsomal monooxygenase P-450 system in the guinea pig and rat. / Kupfer, David; Navarro, Javier.
In: Life Sciences, Vol. 18, No. 5, 01.03.1976, p. 507-513.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Metabolism of prostaglandin A1 by hepatic microsomal monooxygenase P-450 system in the guinea pig and rat
AU - Kupfer, David
AU - Navarro, Javier
PY - 1976/3/1
Y1 - 1976/3/1
N2 - This study demonstrates the metabolic transformation of prostaglandin A1 (PGA1) by guinea pig and rat liver microsomes. The transformation, which required NADPH and oxygen, yielded polar (presumably hydroxylated) products. Incubations with guinea pig liver microsomes yielded one zone of product on tlc, whereas rat liver microsomes produced two discernable metabolic zones. It was demonstrated that PGA1 metabolism in the guinea pig and the rat was inhibited by the addition of SKF-525A, metyrapone, carbon monoxide and cytochrome C; nicotinamide (10 mM) inhibited only the guinea pig system. These findings indicate that the enzymatic activity responsible for PGA1 metabolism is composed of a typical cytochrome P-450 monooxygenase system.
AB - This study demonstrates the metabolic transformation of prostaglandin A1 (PGA1) by guinea pig and rat liver microsomes. The transformation, which required NADPH and oxygen, yielded polar (presumably hydroxylated) products. Incubations with guinea pig liver microsomes yielded one zone of product on tlc, whereas rat liver microsomes produced two discernable metabolic zones. It was demonstrated that PGA1 metabolism in the guinea pig and the rat was inhibited by the addition of SKF-525A, metyrapone, carbon monoxide and cytochrome C; nicotinamide (10 mM) inhibited only the guinea pig system. These findings indicate that the enzymatic activity responsible for PGA1 metabolism is composed of a typical cytochrome P-450 monooxygenase system.
UR - http://www.scopus.com/inward/record.url?scp=0017259160&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0017259160&partnerID=8YFLogxK
U2 - 10.1016/0024-3205(76)90328-3
DO - 10.1016/0024-3205(76)90328-3
M3 - Article
VL - 18
SP - 507
EP - 513
JO - Life Sciences
JF - Life Sciences
SN - 0024-3205
IS - 5
ER -