Thiazolidine-2-carboxylate derivatives formed from glyoxylate and L-cysteine or L-cysteinylglycine as possible physiological substrates for D-aspartate oxidase
- 1 December 1984
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 125 (3) , 1039-1045
- https://doi.org/10.1016/0006-291x(84)91388-3
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- GLUTATHIONEAnnual Review of Biochemistry, 1983
- BIOCHEMISTRY OF SULFUR-CONTAINING AMINO ACIDSAnnual Review of Biochemistry, 1983
- The inhibition of mammalian d-amino acid oxidase by metabolites and drugs. Inferences concerning physiological functionBioorganic Chemistry, 1982
- Inhibition of dopamine β-hydroxylase by thiazoline-2-carboxylate, a suspected physiological product of D-amino acid oxidaseBiochemical and Biophysical Research Communications, 1982
- The mammalian enzyme which replaces b protein of e. coli quinolinate synthetase is d-aspartate oxidaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Thiol-glyoxylate adducts as substrates for rat kidney L-α-hydroxy acid oxidaseBiochemical and Biophysical Research Communications, 1981
- [31] Lipoyl disulfide reducing polymersPublished by Elsevier ,1979
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959
- [49] Determination of glycolic, glyoxylic, and oxalic acidsPublished by Elsevier ,1957
- STUDIES ON THE CYCLOPHORASE SYSTEMPublished by Elsevier ,1949