ArticleThe Histochemical journal1993
In situ kinetic measurements of D-amino acid oxidase in rat liver with respect to its substrate specificity.
Article in The Histochemical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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, 12 citations in OpenAlex.
- In situ heterogeneity of peroxisomal oxidase activities: an update.The Histochemical journal · 1996Review
- Extinction coefficient of polymerized diaminobenzidine complexed with cobalt as final reaction product of histochemical oxidase reactions.Histochemistry and cell biology · 1995Article
- Stereoisomers of cysteine and its analogs Potential effects on chemo- and radioprotection strategies.Amino acids · 1995Article
- Quantitative aspects of enzyme histochemistry on sections of freeze-substituted glycol methacrylate-embedded rat liver.Histochemistry · 1993Article
- Histochemistry of peroxisomal enzyme activities: a tool in the diagnosis of Zellweger syndrome.Journal of inherited metabolic disease · 1993Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
D-Amino acid oxidase activity was demonstrated in peroxisomes of rat liver using unfixed cryostat sections and a histochemical technique using cerium ions as capture reagent for hydrogen peroxide and diaminobenzidine, cobalt ions and exogenous hydrogen peroxide to visualize the final reaction product for light microscopical analysis. Cytophotometric analysis of liver sections revealed similar zero-order reaction velocities of D-amino acid oxidase with activity twice as high in periportal areas as in pericentral areas of liver lobuli when using either D-proline or D,L-thiazolidine-2-carboxylic acid as substrates. On the other hand, a 4-5 times higher KM value was found for D-proline than for D,L-thiazolidine-2-carboxylic acid. The KM values in periportal and pericentral areas were similar for each substrate. These findings support the suggestion that the physiological substrate for D-amino acid oxidase may be D,L-thiazolidine-2-carboxylic acid, the adduct of cysteamine and glyoxylic acid. D-Amino acid oxidase may play a role in vivo in the production of oxalate which may participate in metabolic control processes as an intracellular messenger molecule.
Indexed as
Identifiers
8104917W1980931419What OpenQuestion holds
Registered trials
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