Zellen, Bruce von||Hanzely, Laszlo||Schjeide, Ole A.||Graves, Lynn B.||McCleary, James A.
M.S. (Master of Science)
Department of Biological Sciences
Cell homogenates of Euglena gracilis var. bacillaris (SM-Ll) grown on ethanol had a tenfold higher activity of malate synthase and isocitrate lyase than glucose-grown cells. Fractionation of cell homogenates on a sucrose gradient yielded three distinct fractions: soluble, mitochondrial, and glyoxysomal. The glyoxysome fraction contained malate synthase, isocitrate lyase, glycolate oxidase, and lactate oxidase. However, citrate synthase, malate dehydrogenase, succinate dehydrogenase, and fumarase, usually associated with the mitochondria, were also found at high levels in the glyoxysome fraction. Catalase, which has been reported in all other glyoxysomelike organelles, was not detected. Electron microscopic examination of the glyoxysomal fraction confirmed the presence of these organelles. The primary function of glyoxysomes is gluconeogenesis, however, they also replenish important tricarboxylic acid cycle intermediates which were converted to amino acids for biosynthesis.
Grill, Albin, "Distribution of tricarboxylic acid cycle and glyoxylate by-pass enzymes between Mitochondria and Glyoxysomes of Euglena Gracilis var. Bacillaris (SM-L1)" (1971). Graduate Research Theses & Dissertations. 2269.
Northern Illinois University
Rights Statement 2
NIU theses are protected by copyright. They may be viewed from Huskie Commons for any purpose, but reproduction or distribution in any format is prohibited without the written permission of the authors.