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Cytochemical Localization of Catalase in Glyoxysomes Isolated from Maize Scutella
Author(s) -
Giovanna P. Longo,
Carola Dragonetti,
Claudio P. Longo
Publication year - 1972
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.50.4.463
Subject(s) - glyoxysome , catalase , cytochemistry , biochemistry , organelle , scutellum , peroxidase , membrane , biology , matrix (chemical analysis) , lysis , enzyme , chemistry , glyoxylate cycle , chromatography , endosperm
The localization of catalase in isolated maize scutellum glyoxysomes was investigated by means of the diaminobenzidine histochemical reaction. Only the membranes of the glyoxysomes become heavily stained after incubation with diaminobenzidine and H(2)O(2). If the glyoxysomes are lysed with Tricine buffer at pH 9, 70% of the catalase is solubilized, while the remaining 30% is tightly bound to an insoluble fraction formed mostly by glyoxysomal membranes. This suggests that catalase may be present also in the matrix of the glyoxysomes. The lack of staining of the matrix with diaminobenzidine is probably due to the high concentration of catalase in the membranes of the organelles.

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