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Titolo:
An essential histidine residue in GTP binding domain of bovine brain glutamate dehydrogenase isoproteins
Autore:
Lee, J; Lee, JE; Cho, EH; Choi, SY; 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 Yonsei Univ, Coll Med, Dept Anat, Seoul 120749, South Korea Yonsei Univ Seoul South Korea 120749 ept Anat, Seoul 120749, 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: 12, anno: 2001,
pagine: 121 - 126
SICI:
1016-8478(20010831)12:1<121:AEHRIG>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEUROLOGICAL DISORDERS; SITE; GENE; IDENTIFICATION; ADP;
Keywords:
chemical modification; diethyl pyrocarbonate; glutamate dehydrogenase; GTP binding domain; reactive histidine;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
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:
J. Lee et al., "An essential histidine residue in GTP binding domain of bovine brain glutamate dehydrogenase isoproteins", MOL CELLS, 12(1), 2001, pp. 121-126

Abstract

Greater than 90% of the original activity of the enzymes remained after modification of histidine residues of glutamate dehydrogenase (GDH) isoproteins from bovine brains with diethyl pyrocarbonate (DEPC). This suggests thatthe DEPC modified histidine residues are not critically involved in the catalysis of the GDH isoproteins. The influence of DEPC modified histidine residue(s) on binding of GTP to GDH isoproteins was investigated by protection studies. These studies showed that inhibition of GDH isoproteins by GTP was protected by preincubation of GDH isoproteins with DEPC. The amount of protection was dependent on the concentration of DEPC. The GTP inhibition was fully protected by preincubation of GDH isoproteins with DEPC at saturating concentrations. These results indicate that the histidine residues may play an important role in the GTP binding on GDH isoproteins. Spectrophotometric studies showed that three histidine residues per enzyme subunit were able to react with DEPC in the absence of GTP, whereas two histidine residues per enzyme subunit interacted with DEPC when the enzymes were preincubated with GTP. These results indicate that one of the histidine residues is involved in the GTP binding domain of GDH isoproteins. The quantitative affinity chromatographic studies showed that the influence of GTP on the bindingof GDH isoproteins to DEPC-Sepharose was significantly distinct for the two GDH isoproteins. GDH I was more sensitively affected by GTP than GDH II in the binding affinity for DEPC-Sepharose. ADP, another well-known allosteric regulator, showed no significant changes in the interaction of DEPC withGDH isoproteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 14:40:27