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. 1975 Nov;56(5):710–717. doi: 10.1104/pp.56.5.710

Cytochemical Demonstration of Malate Synthase and Glycolate Oxidase in Microbodies of Cucumber Cotyledons 1

John J Burke a, Richard N Trelease a
PMCID: PMC541905  PMID: 16659378

Abstract

The cytochemical localizations of malate synthase (glyoxysomal marker) and glycolate oxidase (peroxisomal marker) have been examined in cotyledon segments and sucrose-gradient fractions from germinated cucumber (Cucumis sativus L.) seedlings. The seedlings were grown in the dark for 4 days, transferred to 4 hours of continuous light, then returned to the dark for 24 hours. Under these conditions, high specific activities for both glyoxysomal and peroxisomal enzymes are maintained in cotyledon homogenates and microbody-enriched fractions. Electron cytochemistry of the marker enzymes reveals that all or virtually all the microbodies observed in cotyledonary cells and sucrose-gradient fractions contain both enzymes. The staining in gradient fractions was determined from scoring a minimum of 600 photographed microbodies for each enzyme. After correcting for the number of particles stained for catalase reactivity (representing true microbodies), 94 and 97% of the microbodies were found stained for malate synthase and glycolate oxidase activity, respectively.

The results from these studies provide pertinent information toward understanding the succession from glyoxysomal to peroxisomal metabolism in cotyledons of fatty seedlings. The coexistence of two separate microbody types functioning at different stages of development apparently is not the case. The localizations of both marker enzymes within one microbody type strongly suggest that the metabolic transition involves a change in enzyme complement within an ongoing population of microbodies.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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