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Intracellular Localization of Glycolate Dehydrogenase in a Blue-Green Alga ¹

^a Department of Biology, York University, Downsview, M3J 1P3 Ontario, Canada

Glycolate dehydrogenase activity was detected in cell-free extracts of Oscillatoria sp. prepared by osmotic lysis of spheroplasts in 0.05 M potassium phosphate buffer, pH 7.5, containing 0.3 M mannitol. Most of the enzyme activity was found in a particulate fraction and localized in the photosynthetic lamellae after centrifugation in a discontinuous sucrose density gradient. Enzyme activity was detected in this fraction both in the presence and absence of the artificial electron acceptor 2,6-dichlorophenolindophenol (DPIP) and a low rate of O₂ uptake was detected in this lamellar fraction. Activity was lost from the lamellar fraction by repeated washing or by treatment with 0.005% Triton X-100 and the solubilized enzyme activity was DPIP-dependent. The data indicate that both glycolate dehydrogenase and its natural electron acceptor are bound to the photosynthetic lamellae in vivo. In contrast, catalase activity was found in the soluble cytoplasmic fraction.

³ To whom any correspondence should be addressed.

¹ This work was supported by grants from the National Research Council of Canada and was carried out during the tenure of an Ontario Graduate Fellowship to B. G.

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