1972The Journal of ProtozoologyRequires access

Localization of Glyoxylate Cycle Enzymes in Glyoxysomes in Euglena*

Lynn B. Graves, Richard N. Trelease, ALBIN GRILL, Wayne M. Becker

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Abstract

SYNOPSIS. We demonstrated previously microbodies in Euglena gracilis grown in the dark on 2‐carbon substrates. We have now established in Euglena the particulate nature of enzymes known in other organisms to be localized in microbodies (glyoxysomes and leaf peroxisomes). On a linear sucrose gradient the glyoxylate cycle enzymes band together at a nigner equilibrium density (1.20 g/cm3) than mitochondrial marker enzymes (1.17 g/cm3), establishing the existence in Euglena of glyoxysomes similar to those of higher plants. Glyoxylate (hydroxypyruvate) reductase and, under certain conditions, also glycolate dehydrogenase co‐band with the glyoxylate cycle enzymes, suggesting that Euglena glyoxysomes, like those of higher plants, may contain peroxisomal‐type enzymes. Catalase, an enzyme characteristic of microbodies from a variety of sources, was not detected in Euglena.

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SYNOPSIS. We demonstrated previously microbodies in Euglena gracilis grown in the dark on 2‐carbon substrates. We have now established in Euglena the particulate nature of enzymes known in other organisms to be localized in microbodies (glyoxysomes and leaf peroxisomes). On a linear sucrose gradient the glyoxylate cycle enzymes band together at a nigner equilibrium density (1.20 g/cm3) than mitochondrial marker enzymes (1.17 g/cm3), establishing the existence in Euglena of glyoxysomes similar to those of higher plants. Glyoxylate (hydroxypyruvate) reductase and, under certain conditions, also glycolate dehydrogenase co‐band with the glyoxylate cycle enzymes, suggesting that Euglena glyoxysomes, like those of higher plants, may contain peroxisomal‐type enzymes. Catalase, an enzyme characteristic of microbodies from a variety of sources, was not detected in Euglena.

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Available abstract

SYNOPSIS. We demonstrated previously microbodies in Euglena gracilis grown in the dark on 2‐carbon substrates. We have now established in Euglena the particulate nature of enzymes known in other organisms to be localized in microbodies (glyoxysomes and leaf peroxisomes). On a linear sucrose gradient the glyoxylate cycle enzymes band together at a nigner equilibrium density (1.20 g/cm3) than mitochondrial marker enzymes (1.17 g/cm3), establishing the existence in Euglena of glyoxysomes similar to those of higher plants. Glyoxylate (hydroxypyruvate) reductase and, under certain conditions, also glycolate dehydrogenase co‐band with the glyoxylate cycle enzymes, suggesting that Euglena glyoxysomes, like those of higher plants, may contain peroxisomal‐type enzymes. Catalase, an enzyme characteristic of microbodies from a variety of sources, was not detected in Euglena.

Key concepts: Glyoxysome, Glyoxylate cycle, Euglena gracilis, Microbody, Euglena, Peroxisome, Biochemistry, Biology

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