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Titolo:
GLUTAMATE OXIDASE-CATALYZED OXIDATION OF BETA-N-OXALYL-L-ALPHA,BETA-N-DIAMINOPROPIONIC ACID (BETA-ODAP), A NEUROTOXIN IN THE SEEDS OF LATHYRUS-SATIVUS
Autore:
MOGES G; SOLOMON T; JOHANSSON G;
Indirizzi:
LUND UNIV,DEPT ANALYT CHEM,BOX 124 S-22100 LUND SWEDEN UNIV ADDIS ABABA,DEPT CHEM ADDIS ABABA ETHIOPIA
Titolo Testata:
Analytical letters
fascicolo: 12, volume: 27, anno: 1994,
pagine: 2207 - 2221
SICI:
0003-2719(1994)27:12<2207:GOOOB>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
SYSTEM; ALPHA;
Keywords:
BETA-N-OXALYL-L-ALPHA,BETA-DIAMINOPROPIONIC ACID; NEUROTOXIN; LATHYRISM; L-GLUTAMATE OXIDASE; ENZYMATIC OXIDATION; KINETICS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
G. Moges et al., "GLUTAMATE OXIDASE-CATALYZED OXIDATION OF BETA-N-OXALYL-L-ALPHA,BETA-N-DIAMINOPROPIONIC ACID (BETA-ODAP), A NEUROTOXIN IN THE SEEDS OF LATHYRUS-SATIVUS", Analytical letters, 27(12), 1994, pp. 2207-2221

Abstract

Seven enzymes were tested in a screening of catalytic activity towards the neurotoxic L-amino acid, beta-ODAP. L-glutamate oxidase, G1OD, was found to be the only one that showed activity and its kinetic properties were examined by measuring the rate of formation of hydrogen peroxide which was monitored spectrophotometrically at 512 nm, using Trinder's chromogenic reagent. The Michaelis constant, K-M, for the toxin is 0.24 mM at pH 7, comparable with the reported value for glutamate (0.21 mM). The activity of the enzyme was, however, considerably lower (0.78%) than that of the main substrate. Ammonia formation in the reaction was confirmed by the consumption of nicotinamide adenine dinucleotide (NADH) during reduction of alpha-ketoglutarate in presence of L-glutamate dehydrogenase (G1DH) and catalase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 15:58:43