Document Detail

In situ kinetic measurements of D-amino acid oxidase in rat liver with respect to its substrate specificity.
MedLine Citation:
PMID:  8104917     Owner:  NLM     Status:  MEDLINE    
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.
W M Frederiks; C J Van Noorden; F Marx; P T Gallagher; B P Swann
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  The Histochemical journal     Volume:  25     ISSN:  0018-2214     ISO Abbreviation:  Histochem. J.     Publication Date:  1993 Aug 
Date Detail:
Created Date:  1993-11-16     Completed Date:  1993-11-16     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0163161     Medline TA:  Histochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  578-82     Citation Subset:  IM    
Laboratory of Cell Biology and Histology, University of Amsterdam, The Netherlands.
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MeSH Terms
D-Amino-Acid Oxidase / metabolism*
Liver / enzymology*
Proline / analogs & derivatives,  metabolism
Rats, Wistar
Substrate Specificity
Reg. No./Substance:
0/Thiazolidines; 147-85-3/Proline; 16310-13-7/thiazolidine-2-carboxylic acid; EC Oxidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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