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. 1985 Feb;77(2):296–299. doi: 10.1104/pp.77.2.296

Characterization of Peroxisomes from the Alga Bumilleriopsis filiformis1

Wolfgang Gross 1, Uwe Winkler 1, Helmut Stabenau 1
PMCID: PMC1064506  PMID: 16664045

Abstract

The Xanthophycean alga Bumilleriopsis filiformis possesses peroxisomes which on electron micrographs show a mostly spherical or ovoid shape with a diameter in the range of 0.3 micrometer. Their granular matrix is usually of moderate electron density and in a very few cases contains amorphous inclusions. No associations with other organelles could be observed.

During separation in a sucrose gradient, the peroxisomes from Bumilleriopsis equilibrate at a density of 1.22 grams per cubic centimeter. Glycolate oxidase and glyoxylate-glutamate aminotransferase were found in the isolated organelles along with catalase and uricase. However, no further leaf peroxisomal enzymes were detected. This is the first time that an alga of the group of Xanthophyceae has been demonstrated to possess a glycolate oxidase.

The organelles from Bumilleriopsis differ from leaf peroxisomes also by the absence of enzymes of the β-oxidation pathway. All enzymes for the degradation of fatty acids which were tested are located solely in the mitochondria.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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