ArticleThe Histochemical journal1995
A cytophotometric and electron-microscopical study on catalase activity in serial cryostat sections of rat liver.
Article in The Histochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Oxidative stress and antioxidants at biosurfaces: plants, skin, and respiratory tract surfaces.Environmental health perspectives · 1998Review
- L-ascorbic acid metabolism in the ascorbate-deficient arabidopsis mutant vtc1.Plant physiology · 1997Article
- Corticosteroid induction of renal and intestinal K(+)-dependent p-nitrophenylphosphatase in young and adult rats.The Histochemical journal · 1996Article
- In situ heterogeneity of peroxisomal oxidase activities: an update.The Histochemical journal · 1996Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The validity of the histochemical procedure for demonstrating catalase activity in cryostat sections of rat liver at the light- and electron-microscopical level was studied cytophotometrically. Incubations in the presence of 5 mM diaminobenzidine, 44 mM hydrogen peroxide and 2% polyvinyl alcohol performed on fixed cryostat sections resulted in the highest amounts of final reaction product precipitated in a fine granular form which was specific for catalase activity. Serial sections processed for electron microscopy indicated that the osmiophilic final reaction product was exclusively localized in the matrix and core of peroxisomes. The relationship between incubation time and the amounts of final reaction product generated by catalase activity as measured at 460 nm in mid-zonal areas of liver lobules showed non-linearity for the test-minus-control reaction because first-order inactivation of the enzyme occurred during incubation. Linearity of the test-minus-control reaction and section thickness was observed up to 8 microns. Catalase in rat liver showed a Km value of 2.0 mM for its substrate hydrogen peroxide when the diaminobenzidine concentration was 5 mM. It is concluded that the procedure for demonstrating catalase activity in serial cryostat sections of rat liver at the light- and electron-microscopical level is specific and can be applied to quantitative purposes. This approach may be useful in pathology, when only small biopsies are available, when the tissue is heterogeneous, and when other histochemical markers also need to be studied in the same material.
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