LIGHT MICROSCOPIC STUDY OF THE PEROXIDATIC ACTIVITY OF CATALASE IN FORMALDEHYDE-FIXED RAT LIVER
Author(s) -
KeiIchi Hirai
Publication year - 1969
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/17.9.585
Subject(s) - catalase , hydrogen peroxide , chemistry , formaldehyde , staining , formamide , peroxidase , incubation , cytoplasm , biochemistry , peroxisome , parenchyma , organelle , trypsin , enzyme , biology , organic chemistry , genetics , botany , gene
The peroxidatic activity of rat liver catalase was demonstrated by histochemical staining with 3,3'-diaminobenzidine as hydrogen donor. The activity was so weak that its location was hard to identify in formaldehyde-fixed cells, although high catalatic activity was present, as evidenced by the production of bubbles upon the addition of hydrogen peroxide to the incubation medium. Pretreatment of fixed sections for 60 min at 37°C with formamide, urea or trypsin enhanced the peroxidatic activity significantly. The reaction granules scattered throughout the cytoplasm of the parenchymal cells probably correspond to the peroxisomes.
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