Localization of Catalase A in Vacuoles of Saccharomyces cerevisiae: Evidence for the Vacuolar Nature of Isolated "Yeast Peroxisomes"

Localization of Catalase A in Vacuoles of Saccharomyces cerevisiae: Evidence for the Vacuolar... Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 961-970, Juli 1976 Markus SUSANI, Piotr ZIMNIAK, Friederike FESSL and Helmut Ruis Institut für Allgemeine Biochemie der Universität Wien and Ludwig-Boltzmann-Forschungsstelle für Biochemie, Wien (Received 6 May 1976) Summary: The subcellular distribution of catalase A in the yeast Saccharomyces cerevisiae has been investigated. The enzyme was found to be bound to large particles, whereas most of the activity of catalase T was located in a 38 000 g supernatant. Under various isolation conditions catalase A always showed a distribution among subcellular fractions virtually identical to that of two markers for vacuoles, proteinase B and -mannosidase. More than 80 percent of the catalase A activity of a crude vacuole fraction has been detected in purified vacuoles. Malate synthase, isocitrate lyase and glyoxylate reductase (NADP®), three peroxisomal markers, showed a subcellular distribution significantly different from that of catalase A. It is concluded from these results that catalase A is specifically associated with the vacuoles of yeast. Like vacuoles, "peroxisomal" fractions isolated from yeast spheroplasts as described by AversI1! contain only one catalase protein, catalase A. It could be shown by isopycnic and sedimentation velocity separations of crude mitochondrial fractions that catalase A in http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png hoppe-seyler's zeitschrift für physiologische chemie de Gruyter

Localization of Catalase A in Vacuoles of Saccharomyces cerevisiae: Evidence for the Vacuolar Nature of Isolated "Yeast Peroxisomes"

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Publisher
de Gruyter
Copyright
Copyright © 1976 by the
ISSN
0018-4888
eISSN
1437-4315
DOI
10.1515/bchm2.1976.357.2.961
Publisher site
See Article on Publisher Site

Abstract

Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 961-970, Juli 1976 Markus SUSANI, Piotr ZIMNIAK, Friederike FESSL and Helmut Ruis Institut für Allgemeine Biochemie der Universität Wien and Ludwig-Boltzmann-Forschungsstelle für Biochemie, Wien (Received 6 May 1976) Summary: The subcellular distribution of catalase A in the yeast Saccharomyces cerevisiae has been investigated. The enzyme was found to be bound to large particles, whereas most of the activity of catalase T was located in a 38 000 g supernatant. Under various isolation conditions catalase A always showed a distribution among subcellular fractions virtually identical to that of two markers for vacuoles, proteinase B and -mannosidase. More than 80 percent of the catalase A activity of a crude vacuole fraction has been detected in purified vacuoles. Malate synthase, isocitrate lyase and glyoxylate reductase (NADP®), three peroxisomal markers, showed a subcellular distribution significantly different from that of catalase A. It is concluded from these results that catalase A is specifically associated with the vacuoles of yeast. Like vacuoles, "peroxisomal" fractions isolated from yeast spheroplasts as described by AversI1! contain only one catalase protein, catalase A. It could be shown by isopycnic and sedimentation velocity separations of crude mitochondrial fractions that catalase A in

Journal

hoppe-seyler's zeitschrift für physiologische chemiede Gruyter

Published: Jan 1, 1976

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