Enzymatic inactivation of leukotriene B4 by a novel enzyme found in the porcine kidney. Purification and properties of leukotriene B4 12-hydroxydehydrogenase.-Reference-Cited by-同舟云学术

Enzymatic inactivation of leukotriene B4 by a novel enzyme found in the porcine kidney. Purification and properties of leukotriene B4 12-hydroxydehydrogenase.

Published:1993-08 Issue:24 Volume:268 Page:18128-18135
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Yokomizo T.,Izumi T.,Takahashi T.,Kasama T.,Kobayashi Y.,Sato F.,Taketani Y.,Shimizu T.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference53 articles.

1. Leukotriene B ω-Hydroxylase in Rat Liver Microsomes: Identification as a Cytochrome P-450 That Catalyzes Prostaglandin A1 ω-Hydroxylation, and Participation of Cytochrome b5

2. Oxidation of 20-hydroxyleukotriene B4 to 20-carboxyleukotriene B4 by human neutrophil microsomes. Role of aldehyde dehydrogenase and leukotriene B4 omega-hydroxylase (cytochrome P-450LTB omega) in leukotriene B4 omega-oxidation.

3. Characterization of human neutrophil leukotriene B4 omega-hydroxylase as a system involving a unique cytochrome P-450 and NADPH-cytochrome P-450 reductase

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