ArticleThe Journal of cell biology1991
Purification of marginal plates from bovine renal peroxisomes: identification with L-alpha-hydroxyacid oxidase B.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 34 citations in OpenAlex.
- Visualisation of peroxisomes: a journey through seven decades.Histochemistry and cell biology · 2026Review
- Mammalian peroxisomes and reactive oxygen species.Histochemistry and cell biology · 2004Review
- Contributions of the immunogold technique to investigation of the biology of peroxisomes.Histochemistry and cell biology · 1996Review
- Immunocytochemical localization of L-alpha-hydroxyacid oxidase in dense bar of dumb-bell-shaped peroxisomes of monkey kidney.Histochemistry and cell biology · 1995Article
- Immunogold labelling indicates high catalase concentrations in amorphous and crystalline inclusions of sunflower (Helianthus annuus L.) peroxisomes.The Histochemical journal · 1995Article
Corrections and comments
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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
The matrix of mammalian peroxisomes frequently contains crystalline inclusions. The most common inclusions are membrane associated plate-like "marginal plates" of hitherto unknown nature in renal peroxisomes and central polytubular "cores" composed of urate oxidase in hepatic peroxisomes. In bovine kidney, peroxisomes of proximal tubules exhibit peculiar angular shapes that are caused by multiple marginal plates (Zaar, K., and H.D. Fahimi. 1990. Cell Tissue Res. 260:409-414). Enriched or highly purified peroxisome preparations from this source were used to purify and characterize marginal plates. By SDS-PAGE, one major polypeptide of Mr 33,500 was observed that corresponded to the marginal plate protein. This polypeptide was identified by its enzymatic activity as well as by immunoblotting and preembedding immunocytochemistry as the isozyme B of L-alpha-hydroxyacid oxidase (EC 1.4.3.2). Morphologically, marginal plates were revealed to consist of rectangular straight-edged sheets, exhibiting a defined crystalline lattice structure. The sheets apparently are composed of a single layer of protomers which associate laterally to form a plate-like structure. As deduced from the negative staining results and the additional information of the thickness of marginal plates, each protomer seems to consist of eight subunits forming a cube-like array. The tendency of L-alpha-hydroxyacid oxidase B to self-associate in vitro (Philips, D.R., J.A. Duley, D.J. Fennell, and R.S. Holmes. 1976. Biochim. Biophys. Acta. 427:679-687) corresponds to the mode of association of cubical protomers to form the so-called marginal plates in renal peroxisomes.
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