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Occurrence of cytochrome P-450 with prostaglandin omega-hydroxylase activity in rabbit placental microsomes.

Occurrence of cytochrome P-450 with prostaglandin omega-hydroxylase activity in rabbit placental microsomes. Research Abstract Details 

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  • Occurrence of cytochrome P-450 with prostaglandin omega-hydroxylase activity in rabbit placental microsomes. Abstract Text:

    s yamamotoS Yamamoto,e kusunoseE Kusunose,s matsubaraS Matsubara,k ichiharaK Ichihara,m kusunoseM Kusunose,

    The microsomes of placenta and uterus from pregnant rabbits have been found to catalyze the omega-hydroxylation of PGE1, PGE2, PGF2 alpha, and PGA1 as well as the omega- and (omega-1)-hydroxylation of palmitate and myristate in the presence of NADPH. These activities were greatly inhibited by carbon monoxide, indicating the involvement of cytochrome P-450. The apparent Km for PGE1 was 2.38 microM and 2.1 microM with the placental and uterus microsomes, respectively. Cytochrome P-450 has been solubilized with 1% cholate from the placental microsomes, and partially purified by chromatography on 6-amino-n-hexyl Sepharose 4B, DEAE-Sephadex A-50 and hydroxylapatite columns. The partially purified cytochrome P-450 efficiently catalyzed the omega-hydroxylation of various prostaglandins such as PGE1, PGE2, PGF2 alpha, PGD2, and PGA1 in a reconstituted system containing NADPH-cytochrome P-450 reductase, cytochrome b5, and phosphatidylcholine. The reconstituted system also hydroxylated palmitate and myristate at the omega- and (omega-1)-position, but could not hydroxylate laurate. These catalytic properties resemble those of a new form of cytochrome P-450 highly purified from the lung microsomes of progesterone-treated rabbits (Yamamoto, S., Kusunose, E., Ogita, K., Kaku, M., Ichihara, K., and Kusunose, M. (1984) J. Biochem. 96, 593-603). This type of cytochrome P-450, viz., cytochrome P-450 with high prostaglandin omega-hydroxylase activity may play a role in the regulation of prostaglandin levels in pregnancy.

    Occurrence of cytochrome P-450 with prostaglandin omega-hydroxylase activity in rabbit placental microsomes. Publishing Authors By Initials

    s yamamotoS Yamamoto,e kusunoseE Kusunose,s matsubaraS Matsubara,k ichiharaK Ichihara,m kusunoseM 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

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    Occurrence of cytochrome P-450 with prostaglandin omega-hydroxylase activity in rabbit placental microsomes. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 100

    Page Numbers: 175-81

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jul

    YEAR: 1986

    Occurrence of cytochrome P-450 with prostaglandin omega-hydroxylase activity in rabbit placental microsomes. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Occurrence of cytochrome P-450 with prostaglandin omega-hydroxylase activity in rabbit placental microsomes. Keywords Mesh Terms:

    KEYWORDS: Substrate Specificity

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Occurrence of cytochrome P-450 with prostaglandin omega-hydroxylase activity in rabbit placental microsomes. Information

    Substance Name: prostaglandin omega hydroxylases

    Registry Number: EC 1.14.14.1

    Grant and Affiliation Information for Occurrence of cytochrome P-450 with prostaglandin omega-hydroxylase activity in rabbit placental microsomes.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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