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Titolo:
Effects of ADP on different inhibitory properties of brain glutamate dehydrogenase isoproteins by perphenazine.
Autore:
Yoon, HY; Hwang, SH; Lee, EY; Kim, TU; Cho, EH; Cho, SW;
Indirizzi:
Univ Ulsan, Coll Med, Dept Biochem, Songpa Ku, Seoul 138736, South Korea Univ Ulsan Seoul South Korea 138736 Songpa Ku, Seoul 138736, South Korea Yonsei Univ, Coll Hlth Sci, Dept Med Technol, Wonju 222701, South Korea Yonsei Univ Wonju South Korea 222701 Technol, Wonju 222701, South Korea Chosun Univ, Coll Educ, Dept Sci Educ, Kwangju 501759, South Korea Chosun Univ Kwangju South Korea 501759 Educ, Kwangju 501759, South Korea
Titolo Testata:
BIOCHIMIE
fascicolo: 9, volume: 83, anno: 2001,
pagine: 907 - 913
SICI:
0300-9084(200109)83:9<907:EOAODI>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEUROLOGICAL DISORDERS; ANTIPSYCHOTIC-DRUGS; BINDING-SITE; BOVINE BRAIN; LIVER; IDENTIFICATION; PURIFICATION; TISSUES; GENE;
Keywords:
glutamate dehydrogenase; isoenzymes; perphenazine; ADP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Cho, SW Univ Ulsan, Coll Med, Dept Biochem, Songpa Ku, 388-1 Poongnap Dong, Seoul 138736, South Korea Univ Ulsan 388-1 Poongnap Dong Seoul South Korea 138736 uth Korea
Citazione:
H.Y. Yoon et al., "Effects of ADP on different inhibitory properties of brain glutamate dehydrogenase isoproteins by perphenazine.", BIOCHIMIE, 83(9), 2001, pp. 907-913

Abstract

Incubation of glutamate dehydrogenase isoproteins (GDH I and GDH II) from bovine brains with perphenazine resulted in a time-dependent loss of enzymeactivity. 2-Oxoglutarate and NADH, separately or together, gave partial but not complete protection against the inhibition. Although there were no detectable differences between GDH I and GDH II in inhibition by perphenazinein the absence of ADP, the sensitivities to the inhibition by the drug were significantly distinct for the two isoproteins in the presence of ADP. Low concentrations of ADP (0.05-0.20 mM) did not interfere with the inhibition of GDH I and GDH Il by perphenazine. However, in the presence of high concentrations of ADP (0.5-1.0 mM) inhibitory effects of perphenazine on GDH isoproteins were significantly diminished as determined by enzyme kinetics and quantitative affinity chromatography on perphenazine-Sepharose. GDH I was more sensitively reacted with ADP than GDH II on the inhibition by perphenazine. Since physiological ADP levels can vary from 0.05 to > 1.0 mM depending on the rate of oxidative phosphorylation, our results suggest a possibility that two types of GDHs are differently regulated by the antipsychoticactions of perphenazine depending on the physiological concentrations of ADP. GTP and L-leucine, other well-known allosteric regulators, did not affect the inhibitory actions of perphenazine on bovine brain GDH isoproteins. (C) 2001 Societe francaise de biochimie et biologie moleculaire / Editions scientifiques et medicales Elsevier SAS. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 00:25:59