Isolation of peroxisomal enoyl-CoA hydratase in rainbow trout and immunochemical identification with the bifunctional enzyme

Peroxisomes are the sites for β-oxidation of long-chain fatty acids. The peroxisomal bifunctional enzyme (PBE) enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase catalyzes the second and third reactions of the β-oxidation system. Originally termed PPA-80 for peroxisome-proliferation associated 80,...

Full description

Saved in:
Bibliographic Details
Published in:Fish physiology and biochemistry 1990-07, Vol.8 (4), p.347-351
Main Authors: Baldwin, L A, Calabrese, E J, Kostecki, P T, Yang, J H
Format: Article
Language:English
Subjects:
biochemical composition
Brackish
enoyl-CoA hydratase
fatty acids
fish physiology
Freshwater
identification
immunology
Marine
Oncorhynchus mykiss
oxidation
peroxisomes
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Peroxisomes are the sites for β-oxidation of long-chain fatty acids. The peroxisomal bifunctional enzyme (PBE) enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase catalyzes the second and third reactions of the β-oxidation system. Originally termed PPA-80 for peroxisome-proliferation associated 80,000 MW polypeptide, PBE levels are monitored to measure peroxisome proliferation in rodents and other species. The quantity of a 79,000 MW polypeptide in the light mitochondrial fraction of the liver, as analyzed by SDS-PAGE, increases when rainbow trout are exposed to peroxisome proliferating agents. This correlates with increases in acyl-CoA oxidase activity and peroxisome volume density. In the present study, peroxisomal enoyl-CoA hydratase was purified from trout liver and analyzed by immunoblotting with anti-PBE. A positive reaction with the 79,000 MW polypeptide band was observed providing strong evidence that this is the bifunctional enzyme.
ISSN:0920-1742
1573-5168
DOI:10.1007/BF00003430