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Titolo:
Reactive cysteine residue of bovine brain glutamate dehydrogenase isoproteins
Autore:
Cho, SW; Cho, EH; Hwang, SH; Choi, SY;
Indirizzi:
Univ Ulsan, Coll Med, Dept Biochem, Seoul 138736, South Korea Univ Ulsan Seoul South Korea 138736 t Biochem, Seoul 138736, South Korea Chosun Univ, Coll Educ, Dept Sci Educ, Kwangju 501759, South Korea Chosun Univ Kwangju South Korea 501759 Educ, Kwangju 501759, 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:
MOLECULES AND CELLS
fascicolo: 1, volume: 9, anno: 1999,
pagine: 91 - 98
SICI:
1016-8478(19990228)9:1<91:RCROBB>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEGENERATIVE NEUROLOGICAL DISORDERS; RNA-BINDING PROTEIN; ACTIVE-SITE; PYRIDOXAL 5'-PHOSPHATE; MOLECULAR-CLONING; INSULIN RELEASE; HUMAN-LIVER; IDENTIFICATION; SEQUENCE; HYPERAMMONEMIA;
Keywords:
chemical modification; glutamate dehydrogenase isoproteins; peptide mapping; reactive cysteine;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Cho, SW Univ Ulsan, Coll Med, Dept Biochem, Seoul 138736, South Korea UnivUlsan Seoul South Korea 138736 m, Seoul 138736, South Korea
Citazione:
S.W. Cho et al., "Reactive cysteine residue of bovine brain glutamate dehydrogenase isoproteins", MOL CELLS, 9(1), 1999, pp. 91-98

Abstract

Protein chemical studies of glutamate dehydrogenase isoproteins (GDH I andGDH II) from bovine brain reveal that one cystein residue is accessible for reaction with thiol-modifying reagent. Reaction of the two types of GDH isoproteins with p-chloromercuribenzoic acid resulted in a time-dependent loss of enzyme activity. The inactivation followed pseudo first-order kinetics with the second-order rate constant of 83 M-1 s(-1) and 75 M-1 s(-1) for GDH I and GDH II, respectively. The inactivation was partially prevented bypreincubation of the glutamate dehydrogenase isoproteins with NADH. A combination of 10 mM 2-oxoglutarate with 2 mM NADH gave complete protection against the inactivation. There were no significant differences between the two glutamate dehydrogenase isoproteins in their sensitivities to inactivation by p-chloromercuribenzoic indicating that the microenvironmental structures of the GDH isoproteins are very similar to each other. Allosteric effecters such as ADP and GTP had no effects on the inactivation of glutamate dehydrogenase isoproteins by thiol-modifying reagents. By a combination of peptide mapping analysis and labeling with [C-14] p-chloromercuribenzoic acid,a reactive cystein residue was identified as Cys(323) in the overall sequence. The cysteine residue was clearly identical to sequences of other GDH species known.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 19:09:37