Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
CHARACTERIZATION OF THE ENZYMATIC-ACTIVITY FOR BIPHASIC COMPETITION BY GUANOXABENZ 2,6-DICHLOROBENZYLIDENE-AMINO)-3-HYDROXYGUANIDINE) AT ALPHA(2)-ADRENOCEPTORS II - DESCRIPTION OF A XANTHINE-DEPENDENT ENZYMATIC-ACTIVITY IN SPLEEN CYTOSOL
Autore:
DAMBROVA M; UHLEN S; WELCH CJ; PRUSIS P; WIKBERG JES;
Indirizzi:
BMC,BOX 591 SE-75124 UPPSALA SWEDEN UPPSALA UNIV,DEPT PHARMACEUT BIOSCI,DIV PHARMACOL UPPSALA SWEDEN UPPSALA UNIV,DIV ORGAN CHEM,DEPT PHARMACEUT CHEM UPPSALA SWEDEN
Titolo Testata:
Biochemical pharmacology
fascicolo: 9, volume: 56, anno: 1998,
pagine: 1121 - 1128
SICI:
0006-2952(1998)56:9<1121:COTEFB>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
RADIOLIGAND BINDING; N-HYDROXYLATION; RAT-KIDNEY; 2 FORMS; SUBTYPES; ALPHA-2B-ADRENOCEPTORS; ALPHA-2-ADRENOCEPTOR; DELINEATION; METABOLITE; GUANABENZ;
Keywords:
N-HYDROXYGUANIDINE; GUANOXABENZ; METABOLIC CONVERSION; REDUCTION; SPLEEN; XANTHINE OXIDASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
M. Dambrova et al., "CHARACTERIZATION OF THE ENZYMATIC-ACTIVITY FOR BIPHASIC COMPETITION BY GUANOXABENZ 2,6-DICHLOROBENZYLIDENE-AMINO)-3-HYDROXYGUANIDINE) AT ALPHA(2)-ADRENOCEPTORS II - DESCRIPTION OF A XANTHINE-DEPENDENT ENZYMATIC-ACTIVITY IN SPLEEN CYTOSOL", Biochemical pharmacology, 56(9), 1998, pp. 1121-1128

Abstract

The mechanism for formation of high affinity binding of guanoxabenz 2,6-dichlorobenzylidene-amino)-3-hydroxyguanidine) to alpha(2)-adrenoceptors by the rat spleen cytosol was studied. We report here that the spleen cytosolic fraction mediated the reduction of guanoxabenz to nz(1-(2,6-dichlorobenzylidene-amino)-3-guanidine), the latter having an almost 100-fold higher affinity for rat alpha(2A)-adrenoceptors than guanoxabenz itself. The reaction product could be separated by high-performance liquid chromatography and its identity as guanabenz confirmed by nuclear magnetic resonance. The spleen cytosolic activity could be separated into high and low molecular weight components, the high molecular weight component requiring low molecular weight factors for maximal activity. Xanthine oxidase seems to be the most likely candidate responsible for the activity, as the guanoxabenz-reducing activity of the high molecular weight component could be sustained by exogenously applied xanthine, while it was potently blocked by allopurinol. The conversion of guanoxabenz by the cytosolic activity was also quite potently blocked by DWO1, (3,4-dimethoxybenzylideneamino)3-hydroxyguanidine, a hydroxyguanidine analogue to guanoxabenz. (C) 1998 Elsevier Science Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 04:28:24