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Titolo:
Identification of lysine residue involved in inactivation of brain glutamate dehydrogenase isoproteins by o-phthalaldehyde
Autore:
Ahn, JY; Choi, S; Cho, SW;
Indirizzi:
Univ Ulsan, Coll Med, Dept Biochem, Seoul 138736, South Korea Univ Ulsan Seoul South Korea 138736 t Biochem, Seoul 138736, South Korea Hallym Univ, Dept Genet Engn, Div Life Sci, Chunchon 200702, South Korea Hallym Univ Chunchon South Korea 200702 ci, Chunchon 200702, South Korea
Titolo Testata:
BIOCHIMIE
fascicolo: 12, volume: 81, anno: 1999,
pagine: 1123 - 1129
SICI:
0300-9084(199912)81:12<1123:IOLRII>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
BOVINE LIVER; PYRIDOXAL 5'-PHOSPHATE; NEUROLOGICAL DISORDERS; BINDING-SITE; ACTIVE-SITE; SEQUENCE; CYSTEINE; ENZYME;
Keywords:
glutamate dehydrogenase; o-phthalaldehyde; reactive lysine; peptide mapping;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Cho, SW Univ Ulsan, Coll Med, Dept Biochem, 388-1 Poongnap Dong, Seoul 138736, South Korea Univ Ulsan 388-1 Poongnap Dong Seoul South Korea 138736 uth Korea
Citazione:
J.Y. Ahn et al., "Identification of lysine residue involved in inactivation of brain glutamate dehydrogenase isoproteins by o-phthalaldehyde", BIOCHIMIE, 81(12), 1999, pp. 1123-1129

Abstract

Incubation of two types of glutamate dehydrogenase (GDH) isoproteins from bovine brain with o-phthalaldehyde resulted in a time-dependent loss of enzyme activity. The inactivation was partially prevented by preincubation of the GDH isoproteins with 2-oxoglutarate or NADH. Spectrophotometric studiesindicated that the inactivation of GDH isoproteins with o-phthalaldehyde resulted in isoindole derivatives characterized by typical fluorescence emission spectra with a stoichiometry of one isoindole derivative per molecule of enzyme subunit. There were no differences between the two GDH isoproteins in sensitivities to inactivation by o-phthalaldehyde indicating that the microenvironmental structures of the GDH isoproteins are very similar to each other. Tryptic peptides of the isoproteins, modified with and without protection, identified a selective modification of one lysine as in the region containing the sequence L-Q-H-G-S-I-L-G-F-P-(X) under bar-A-K for both GDH isoproteins. The symbol (X) under bar indicates a position for which no phenylthiohydantoin-amino acid could be assigned. The missing residue, however, can be designated as an o-phthalaldehyde-labeled lysine since the sequences including the lysine residue in question have a complete identity withthose of the other mammalian GDHs. Also, trypsin was unable to cleave the labeled peptide at this site. Both amino acid sequencing and compositional analysis identified Lys-306 as the site of o-phthalaldehyde binding within the brain GDH isoproteins. (C) Society francaise de biochimie et biologie moleculaire/Editions scientifiques et medicales Elsevier SAS.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 20:22:40