Abstract
In this paper we report on the subcellular localization of peroxisomal thiolase in rat liver using density-gradient centrifugation and immunoelectron microscopy. The results obtained show that peroxisomes display great biochemical heterogeneity and can not be regarded as one homogeneous population of particles. We conclude that rat liver contains at least three distinct populations of peroxisomes, which are present both in normal-fed rats as well in rats treated with a plasticizer, di-(2-ethylhexyl)phthalate, known to induce peroxisomes. The following types of peroxisomes could be discerned: (1) Low-density peroxisomal particles containing 69-kDa peroxisomal membrane protein (PMP), dihydroxyacetonephosphate acyltransferase (DHAPAT) and the precursor form of peroxisomal thiolase (44-kDa). (2) Intermediate-density peroxisomal particles containing 69-kDa peroxisomal membrane protein, dihydroxyacetonephosphate acyltransferase, both 41-kDa (mature) and 44-kDa (immature) peroxisomal thiolase, catalase and d-aminoacid oxidase. (3) High-density peroxisomes containing 69-kDa peroxisomal membrane protein, dihydroxyacetonephosphate acyltransferase, 41-kDa thiolase, catalase and d-aminoacid oxidase.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - General Subjects
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