ArticleHistochemistry1985
Light and electron microscopic localization of L-alpha-hydroxyacid oxidase in rat kidney revealed by immunocytochemical techniques.
Article in Histochemistry, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 30 citations in OpenAlex.
- A brief history of the human liver peroxisome.Histochemistry and cell biology · 2026Review
- In situ heterogeneity of peroxisomal oxidase activities: an update.The Histochemical journal · 1996Review
- Immunocytochemical localization of L-alpha-hydroxyacid oxidase in dense bar of dumb-bell-shaped peroxisomes of monkey kidney.Histochemistry and cell biology · 1995Article
- L-2-hydroxyglutaric acidaemia: clinical and biochemical findings in 12 patients and preliminary report on L-2-hydroxyacid dehydrogenase.Journal of inherited metabolic disease · 1993Article
- Import of proteins into peroxisomes and other microbodies.The Biochemical journal · 1992Review
- Purification of marginal plates from bovine renal peroxisomes: identification with L-alpha-hydroxyacid oxidase B.The Journal of cell biology · 1991Article
- Article
- A new method of the immunohistochemical detection of cellular antigens for light and electron microscopy.Histochemistry · 1989Article
- Immunoelectron microscopic localization of D-amino acid oxidase in rat kidney and liver.The Histochemical journal · 1987Article
- Electron microscopic cytochemical localization of alpha-hydroxyacid oxidase in rat kidney cortex. Heterogeneous staining of peroxisomes.Histochemistry · 1986Article
- Immunocytochemical demonstration of serine: pyruvate amino-transferase in peroxisomes and mitochondria of rat kidney.Histochemistry · 1985Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Light and electron microscopic localization of L-alpha-hydroxyacid oxidase (L-HOX) in rat kidney was studied by means of immunocytochemical techniques. Isozymes A and B of L-HOX were purified from rat liver and kidney, respectively. The apparent molecular weights of the subunits of the isozymes A and B were 35,800 and 33,500 daltons, respectively, by a slab gel electrophoresis. Antibodies to the isozymes were raised in rabbits. Anti(isozyme A) is not cross-reactive with the isozyme B and vice versa anti(isozyme B) not with the isozyme A. Using anti-isozyme B, semithin sections of Epon-embedded material and ultrathin sections of Lowicryl K4M-embedded material were stained by immunoenzyme and protein A-gold techniques, respectively. By light microscopy, fine discrete granular staining was noted in proximal tubules, but not in distal tubules including thick and thin limbs of Henle and collecting tubules. By electron microscopy, gold particles representing the antigen sites for L-HOX B were confined exclusively to peroxisomes, in which most of the gold particles were localized in electron dense peripheral matrix, but little in central matrix with low electron density. The results indicate that L-HOX B does not homogeneously distribute in peroxisomes of rat kidney but might be associated with some substructure within peroxisome matrix.
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