Isolation of cytochrome P-450 highly active in prostaglandin omega-hydroxylation from lung microsomes of rabbits treated with progesterone.

Isolation of cytochrome P-450 highly active in prostaglandin omega-hydroxylation from lung microsomes of rabbits treated with progesterone. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Isolation of cytochrome P-450 highly active in prostaglandin omega-hydroxylation from lung microsomes of rabbits treated with progesterone. Abstract Text:

S Yamamoto,E Kusunose,K Ogita,M Kaku,K Ichihara,M Kusunose,

Two forms of cytochrome P-450, designated as cytochrome P-450p-1 and cytochrome P-450p-2, were separated and purified to specific contents of 8.2 and 8.9 nmol/mg of protein, respectively, from lung microsomes of rabbits treated with progesterone. Cytochrome P-450p-1 and cytochrome P-450p-2 migrated as single polypeptide bands with molecular weights of 49,000 and 52,000, respectively, on SDS-polyacrylamide gel. Their CO-reduced difference spectral peaks were at 451.5 and 450 nm, respectively. Cytochrome P-450p-1 catalyzed the N-demethylation of benzphetamine, O-demethylation of p-nitroanisole, and O-deethylation of 7-ethoxycoumarin, whereas no activity was observed with cytochrome P-450p-2. On the other hand, cytochrome P-450p-2 catalyzed the omega-hydroxylation of prostaglandin E1 (PGE1), prostaglandin E2 (PGE2), and prostaglandin A1 (PGA1) with turnover rates of 9.0, 7.5, and 5.0 nmol of product/min/nmol of cytochrome P-450, respectively, as well as the omega- and (omega-1)-hydroxylation of palmitate and myristate with turnover rates of 27.7 and 16.4 nmol products/min/nmol of cytochrome P-450, respectively. This cytochrome showed a greater affinity for prostaglandins (PGs) than for fatty acids. These reactions were absolutely dependent on cytochrome P-450p-2 and NADPH-cytochrome P-450 reductase, and stimulated by addition of phosphatidylcholine and cytochrome b5. Cytochrome P-450p-2 is thought to be a new form of cytochrome P-450 induced by progesterone treatment in rabbit lung microsomes.

Isolation of cytochrome P-450 highly active in prostaglandin omega-hydroxylation from lung microsomes of rabbits treated with progesterone. Publishing Authors By Initials

S Yamamoto,E Kusunose,K Ogita,M Kaku,K Ichihara,M Kusunose,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

PUBMED ID PMID:

MEDLINE DATE:

Isolation of cytochrome P-450 highly active in prostaglandin omega-hydroxylation from lung microsomes of rabbits treated with progesterone. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 96

Page Numbers: 593-603

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 1984

Isolation of cytochrome P-450 highly active in prostaglandin omega-hydroxylation from lung microsomes of rabbits treated with progesterone. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Isolation of cytochrome P-450 highly active in prostaglandin omega-hydroxylation from lung microsomes of rabbits treated with progesterone. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: metabolism

Chemical & Substance for Abstract: Isolation of cytochrome P-450 highly active in prostaglandin omega-hydroxylation from lung microsomes of rabbits treated with progesterone. Information

Substance Name: Mixed Function Oxygenases

Registry Number: EC 1.-

Grant and Affiliation Information for Isolation of cytochrome P-450 highly active in prostaglandin omega-hydroxylation from lung microsomes of rabbits treated with progesterone.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Isolation of cytochrome P-450 highly active in prostaglandin omega-hydroxylation from lung microsomes of rabbits treated with progesterone 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.