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Titolo:
Equilibrium in the hydrolysis and synthesis of cannabimimetic anandamide demonstrated by a purified enzyme
Autore:
Katayama, K; Ueda, N; Katoh, I; Yamamoto, S;
Indirizzi:
Univ Tokushima, Sch Med, Dept Cardiovasc Surg, Tokushima 7708503, Japan Univ Tokushima Tokushima Japan 7708503 sc Surg, Tokushima 7708503, Japan
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
fascicolo: 2-3, volume: 1440, anno: 1999,
pagine: 205 - 214
SICI:
1388-1981(19990922)1440:2-3<205:EITHAS>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
CANNABINOID RECEPTOR AGONIST; RAT-BRAIN MICROSOMES; ACID AMIDE HYDROLASE; N-ARACHIDONOYLETHANOLAMINE; ENDOGENOUS LIGAND; ARACHIDONIC-ACID; AMIDOHYDROLASE; IDENTIFICATION; DERIVATIVES; BINDING;
Keywords:
anandamide; arachidonic acid; cannabinoid; amidohydrolase; palmitoylethanolamide; equilibrium constant;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Yamamoto, S Univ Tokushima, Sch Med, Dept Cardiovasc Surg, Tokushima 7708503, Japan Univ Tokushima Tokushima Japan 7708503 ushima 7708503, Japan
Citazione:
K. Katayama et al., "Equilibrium in the hydrolysis and synthesis of cannabimimetic anandamide demonstrated by a purified enzyme", BBA-MOL C B, 1440(2-3), 1999, pp. 205-214

Abstract

Anandamide, an endogenous ligand for cannabinoid receptors, loses its biological activities when it is hydrolyzed to arachidonic acid and ethanolamine by anandamide amidohydrolase. We overexpressed a recombinant rat enzyme with a hexahistidine tag in a baculovirus-insect cell expression system, andpurified the enzyme with the aid of a Ni-charged resin to a specific activity as high as 5.7 mu mol/min/mg protein. The purified recombinant enzyme catalyzed not only the hydrolysis of anandamide and palmitoylethanolamide, but also their reverse synthetic reactions. In order to attain an equilibrium of the anandamide hydrolysis and its reverse reaction within 10 min, we utilized a large amount of the purified enzyme. The equilibrium constant([arachidonicacid][ethanolamine])/ ([anandamide][water]) was calculated as 4 X 10(-3) (37 degrees C, pH 9.0). These experimental results with a purified enzyme preparation quantitatively confirmed the reversibility of the enzyme reaction previously observed with crude enzyme preparations. (C) 1999 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 15:45:31