Isolation and characterization of peroxisomes from diatoms

✍ Scribed by U. Winkler; H. Stabenau

• Publisher: Springer-Verlag
• Year: 1995
• Tongue: English
• Weight: 628 KB
• Volume: 195
• Category: Article
• ISSN: 0032-0935
• DOI: 10.1007/bf00202598

✦ Synopsis

Peroxisomes were isolated by gradient centrifugation from two different diatoms: Nitzschia laevis (subgroup of Pennales) and Thalassiosirafluviatilis (subgroup of Centrales). In neither of these organelles could catalase or any H202-forming oxidase be demonstrated. The glycolate-oxidizing enzyme present in the peroxisomes is a dehydrogenase capable of oxidizing L-lactate as well. The peroxisomes also contain the glyoxysomal markers isocitrate lyase and malate synthase. However, enzymes of the fatty-acid [3-oxidation pathway are located exclusively in the mitochondria. The mitochondria additionally possess glutamate-glyoxylate aminotransferase and a glycolate dehydrogenase which differs from the peroxisomal glycolate dehydrogenase since it preferably utilizes o-lactate as an alternative substrate. Hydroxypyruvate reductase and glyoxylate carboligase were not found in the cells of either diatom. By culturing Nitzschia laevis it could be demonstrated that decreasing the CO 2 concentration in the aeration mixture from 2% to 0.03% and increasing the irradiance from 40 to 250 pmol quanta.m -2. s -1 resulted in an increase of all peroxisomal enzyme activities. In addition, enzyme activities of the [3-oxidation pathway were increased. However, mitochondrial glycolate dehydrogenase and aminotransferase did not alter their activities under these conditions. Summarizing all results, it is postulated that there are two different pathways for the metabolism of glycolate in the diatoms.