In situ kinetic measurements of d-amino acid oxidase in rat liver with respect to its substrate specificity
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Anatomy
Link
http://link.springer.com/content/pdf/10.1007/BF00173056.pdf
Reference25 articles.
1. Angermüller, S. & Fahimi, H. D. (1988a) Heterogenous staining of d-amino acid oxidase in peroxisomes of rat liver and kidney. A light and electron microscopic study. Histochemistry 88, 277?85.
2. Angermüller, S. & Fahimi, H. D. (1988b) Light microscopic visualization of the reaction product of cerium used for localization of peroxisomal oxidases. J. Histochem. Cytochem. 36, 23?8.
3. Briggs, R. T., Drath, D. B., Karnovsky, M. L. & Karnovsky, M. J. (1975) Localization of NADH oxidase on the surface of human polymorphonuclear leukocytes by a new cytochemical method. J. Cell. Biol. 67, 566?86.
4. Dixon, M. & Kleppe, K. (1965) d-Amino acid oxidase. II. Specificity, competitive inhibition and reaction sequence. Biochim. Biophys. Acta 96, 368?82.
5. Fitzpatrick, P. F. & Massey, V. (1982) Thiazolidine-2-carboxylic acid, an adduct of cysteamine and glyoxalate, as a substrate for d-amino acid oxidase. J. Biol. Chem. 257, 1166?71.
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