Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Plant Physiology 77:296-299 (1985)
© 1985 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gross, W.
Right arrow Articles by Stabenau, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gross, W.
Right arrow Articles by Stabenau, H.
Agricola
Right arrow Articles by Gross, W.
Right arrow Articles by Stabenau, H.
Articles

Characterization of Peroxisomes from the Alga Bumilleriopsis filiformis1

Wolfgang Gross, Uwe Winkler and Helmut Stabenau

Universität Oldenburg, Fachbereich Biologie, Postfach 2503, D-2900 Oldenburg, West Germany

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 beta-oxidation pathway. All enzymes for the degradation of fatty acids which were tested are located solely in the mitochondria.


1 Supported by the Deutsche Forschungsgemeinschaft.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1985 by the American Society of Plant Biologists