Hydroxylation of prostaglandin A1 by the microsomes of rabbit intestinal mucosa.

Hydroxylation of prostaglandin A1 by the microsomes of rabbit intestinal mucosa. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Hydroxylation of prostaglandin A1 by the microsomes of rabbit intestinal mucosa. Abstract Text:

E Kusunose,M Kaku,K Ichihara,S Yamamoto,I Yano,M Kusunose,

Microsomes from rabbit small intestine mucosa were found to catalyze the hydroxylation of PGA1 in the presence of NADPH. The major product was identified as 20-hydroxy PGA1 by using high performance liquid chromatography and gas chromatography-mass spectrometry, and the minor product was assumed to be 19-hydroxy PGA1. The ratio of the former product to the latter was about 24.1. The specific PGA1 omega-hydroxylase activity of small intestine microsomes was comparable to that of liver microsomes, and was significantly higher than those of microsomes from other tissues such as kidney cortex and lung. Microsomes from rabbit colon mucosa also catalyzed the hydroxylation of PGA1 in the presence of NADPH, with the ratio of omega- to (omega-1)-hydroxy PGA1 formed being 33.0. The PGA1 hydroxylase activities of the microsomes from both small intestine and colon were inhibited markedly by carbon monoxide, indicating the participation of cytochrome P-450. A cytochrome P-450 was solubilized from small intestine microsomes, and purified to a specific content of 10.5 nmol of cytochrome P-450/mg of protein. This cytochrome hydroxylated PGA1 at the omega-position with a turnover rate of 38.2 nmol/min/nmol of cytochrome P-450 in the reconstituted system containing cytochrome P-450, NADPH-cytochrome P-450 reductase, cytochrome b5 and phosphatidylcholine. It is suggested that this cytochrome P-450 is specialized for the omega-hydroxylation of PGA1 in small intestine microsomes.

Hydroxylation of prostaglandin A1 by the microsomes of rabbit intestinal mucosa. Publishing Authors By Initials

E Kusunose,M Kaku,K Ichihara,S Yamamoto,I Yano,M Kusunose,

For similar animals: chordata: vertebrates: mammals: lagomorpha: rabbits research abstracts see: animals: chordata: vertebrates: mammals: lagomorpha: rabbits research

PUBMED ID PMID:

MEDLINE DATE:

Hydroxylation of prostaglandin A1 by the microsomes of rabbit intestinal mucosa. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 95

Page Numbers: 1733-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jun

YEAR: 1984

Hydroxylation of prostaglandin A1 by the microsomes of rabbit intestinal mucosa. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Hydroxylation of prostaglandin A1 by the microsomes of rabbit intestinal mucosa. Keywords Mesh Terms:

KEYWORDS: Rabbits

MESH TERMS: metabolism

Chemical & Substance for Abstract: Hydroxylation of prostaglandin A1 by the microsomes of rabbit intestinal mucosa. Information

Substance Name: prostaglandin omega hydroxylases

Registry Number: EC 1.14.14.1

Grant and Affiliation Information for Hydroxylation of prostaglandin A1 by the microsomes of rabbit intestinal mucosa.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Hydroxylation of prostaglandin A1 by the microsomes of rabbit intestinal mucosa Related Publications

• BF(2) complexes of alpha-alkyl-substituted dipyrrolyldiketones as acyclic anion receptors.
• Characterization of human liver leukotriene B(4) omega-hydroxylase P450 (CYP4F2).
• Different mechanisms of regioselection of fatty acid hydroxylation by laurate (omega-1)-hydroxylating P450s, P450 2C2 and P450 2E1.
• Effect of cytochrome b5 on fatty acid omega- and (omega-1)-hydroxylation catalyzed by partially purified cytochrome P-450 from rabbit kidney cortex microsomes.
• Effect of peroxisomal proliferators on microsomal prostaglandin A omega-hydroxylase.
• Fatty acid omega and (omega-1)-Hydroxylation in rabbit intestinal mucosa microsomes.
• Hydroxylation of prostaglandin A1 by the microsomes of rabbit intestinal mucosa.
• Incorporation of radioactivity from methionine-methyl-14C into phospholipids by Nocardia polychromogenes.
• Isolation of a new form of cytochrome P-450 with prostaglandin A and fatty acid omega-hydroxylase activities from rabbit kidney cortex microsomes.
• Isolation of cytochrome P-450 highly active in prostaglandin omega-hydroxylation from lung microsomes of rabbits treated with progesterone.
• Multiple forms of cytochrome P-450 in kidney cortex microsomes of rabbits treated with 3-methylcholanthrene.
• Occurrence of cytochrome P-450 with prostaglandin omega-hydroxylase activity in rabbit placental microsomes.
• Partial purification of a carbon monoxide-binding hemoprotein reconstitutively active in fatty acid omega-hydroxylation from porcine kidney cortex microsomes.
• Purification and cDNA cloning of human liver CYP4A fatty acid omega-hydroxylase.
• Purification and characterization of cytochrome P-450 specific for prostaglandin and fatty acid hydroxylase activities from the microsomes of rabbit small intestinal mucosa.
• Purification and characterization of hepatic microsomal prostaglandin omega-hydroxylase cytochrome P-450 from pregnant rabbits.
• Purification and characterization of two forms of cytochrome P-450 with omega-hydroxylase activities toward prostaglandin A and fatty acids from rabbit liver microsomes.
• Purification and characterization of two forms of fatty acid omega-hydroxylase cytochrome P-450 from rabbit kidney cortex microsomes.
• Reconstruction of aryl hydrocarbon hydroxylase from rabbit intestinal mucosa microsomes.
• Replacement of Thr-303 of P450 2E1 with serine modifies the regioselectivity of its fatty acid hydroxylase activity.
• Some properties of a hexadecane hydroxylation system in rabbit intestinal mucosa microsomes.
• Superoxide dismutase from Mycobacterium tuberculosis.