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Microperoxisomes in the epithelial cells of the amphibian urinary bladder: an electron microscopic demonstration of catalase and malate synthase.
Author(s) -
Ruth G. Jones,
Wendy Davis,
David B. P. Goodman
Publication year - 1981
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/29.10.6795257
Subject(s) - malate synthase , toad , malate dehydrogenase , organelle , catalase , peroxisome , urinary bladder , biology , glyoxylate cycle , atp synthase , epithelium , enzyme , chemistry , mitochondrion , biochemistry , endocrinology , medicine , isocitrate lyase , genetics , gene
All cells that comprise the epithelium of the toad urinary bladder were found to contain small ovoid to tubular membrane-bound bodies with a finely granular matrix. Such organelles were devoid of dense cores (nucleoids). These microperoxisomes reacted positively when incubated for the demonstration of catalase or malate synthase activity. In the toad liver, peroxisomes as well as microperoxisomes were seen. Histochemically, both demonstrated catalase activity; neither showed malate synthase activity. The presence of malate synthase, a glyoxylate cycle enzyme, in toad urinary bladder microperoxisomes may make these latter organelles unique among vertebrates, since malate synthase has been thought to be absent in higher animals.

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