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Titolo:
CO-SOLUBILIZATION OF BRADYKININ B-2 RECEPTORS AND ANGIOTENSIN-CONVERTING ENZYME FROM GUINEA-PIG LUNG MEMBRANES
Autore:
TRIFILIEFF A; LACH E; MOUSLI M; HADDAD EB; LANDRY Y; GIES JP;
Indirizzi:
UNIV LOUIS PASTEUR STRASBOURG 1,INSERM,CJF 9105,NEUROIMMUNOPHARMACOL LAB,BP 24 F-67401 ILLKIRCH GRAFFENS FRANCE UNIV LOUIS PASTEUR STRASBOURG 1,INSERM,CJF 9105,NEUROIMMUNOPHARMACOL LAB F-67401 ILLKIRCH GRAFFENS FRANCE
Titolo Testata:
Biochimica et biophysica acta. Biomembranes
fascicolo: 1, volume: 1191, anno: 1994,
pagine: 109 - 116
SICI:
0005-2736(1994)1191:1<109:COBBRA>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
BINDING-SITES; NG108-15 CELLS; PERTUSSIS TOXIN; RAT; ANTAGONISTS; PROTEINS; CLONING; KININS; BRAIN;
Keywords:
BRADYKININ RECEPTOR; ANGIOTENSIN-CONVERTING ENZYME; SOLUBILIZATION; [H-3] BRADYKININ BINDING; LUNG; (GUINEA PIG);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
A. Trifilieff et al., "CO-SOLUBILIZATION OF BRADYKININ B-2 RECEPTORS AND ANGIOTENSIN-CONVERTING ENZYME FROM GUINEA-PIG LUNG MEMBRANES", Biochimica et biophysica acta. Biomembranes, 1191(1), 1994, pp. 109-116

Abstract

Bradykinin B-2 receptor-like binding activity was solubilized from guinea pig lung using the zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propa (Chaps). The binding of [H-3]bradykinin to thesoluble fraction was time-dependent and saturable. Scatchard analysisof equilibrium binding data indicated that the soluble extract contained a single class of binding sites with a K-d Of 696 pM and a B-max of 57 fmol/mg protein. Unlabelled bradykinin and B-2 antagonists inhibited the binding of [H-3]bradykinin to Chaps-solubilized extracts with relative potencies similar to those observed with the low-affinity membrane-bound binding sites. Following partial purification of the soluble preparation, using anion exchange (DEAE-Sephacel) and gel filtration (Aca 34) column chromatography steps, two peaks eluted off the column were able to bind [H-3]bradykinin and have molecular masses of 168 and 98.5 kDa. The former seems to represent binding of bradykinin to angiotensin converting enzyme (ACE, EC 3.4.15.1) and the latter binding to bradykinin receptor. Using purified commercial ACE, we show that the binding of [H-3]bradykinin to ACE can easily be distinguished from that of the bradykinin receptor, since both B-1 and B-2 ligands were able to inhibit bradykinin binding with affinities clearly different from that expected for a bradykinin receptor.

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Documento generato il 30/10/20 alle ore 23:25:38