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Titolo:
IDENTIFICATION AND CHARACTERIZATION OF A NEUTRAL ENDOPEPTIDASE ACTIVITY IN APLYSIA-CALIFORNICA
Autore:
BAWAB W; ALOYZ RS; CRINE P; ROQUES BP; DESGROSEILLERS L;
Indirizzi:
UNIV MONTREAL,DEPT BIOCHEM,POB 6128,STN A MONTREAL H3C 3J7 QUEBEC CANADA UNIV MONTREAL,DEPT BIOCHEM,POB 6128,STN A MONTREAL H3C 3J7 QUEBEC CANADA UNIV PARIS 05,UFR SCI PHARMACEUT & BIOL,DEPT CHIM ORGAN,CNRS,URA 498,INSERM,U266 F-75270 PARIS 06 FRANCE
Titolo Testata:
Biochemical journal
, volume: 296, anno: 1993,
parte:, 2
pagine: 459 - 465
SICI:
0264-6021(1993)296:<459:IACOAN>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
BAG CELL PEPTIDE; ENKEPHALIN-DEGRADING PEPTIDASE; LOCUST SCHISTOCERCA-GREGARIA; AMINOPEPTIDASE-LIKE ACTIVITY; KIDNEY BRUSH-BORDER; AMINO-ACID SEQUENCE; RAT-BRAIN; MONOCLONAL-ANTIBODY; 24.11 ENKEPHALINASE; RENAL DIPEPTIDASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
W. Bawab et al., "IDENTIFICATION AND CHARACTERIZATION OF A NEUTRAL ENDOPEPTIDASE ACTIVITY IN APLYSIA-CALIFORNICA", Biochemical journal, 296, 1993, pp. 459-465

Abstract

Kidney plasma membranes of Aplysia californica were shown to contain an endopeptidase activity which cleaved [Leu]enkephalin (Tyr-Gly-Gly-Phe-Leu) and [Leu]enkephalinamide (Tyr-Gly-Gly-Phe-Leu-NH2) at the Gly3-Phe4 bond, as determined by reverse-phase h.p.l.c. analysis of metabolites. The optimal pH was shown to be 6.5. The bivalent cation chelating agent 1,10-phenanthroline protected [Leu]enkephalin from degradation, suggesting that this enzyme is a metallopeptidase. The degradation of [Leu]enkephalin was also abolished by the neutral endopeptidase-24.11 inhibitors RB104 o-3-oxo-1-phenylmethyl)-propyl]amino-4-oxobutanoicacid), HABCO-Gly droxy-aminocarbonyl-2-benzyl-1-oxypropyl)glycine], phosphoramidon and thiorphan, with IC50 values of 1 nM, 1 muM, 20 muM and 30 muM respectively. By contrast, the angiotensin-converting enzymeinhibitor captopril and the serine proteinase inhibitor phenylmethanesulphonyl fluoride were without effect. Phase separation experiments using Triton X-114 showed that about 64% of the neutral endopeptidase activity in the Aplysia kidney membrane corresponds to an integral membrane protein. A specific radioiodinated inhibitor ([I-125]RB 104) was shown to bind the Aplysia endopeptidase with high affinity; the K(D) and B(max) values were 21+/-5 pM and 20.3+/-5 fmol/mg of proteins respectively. This inhibitor was used to determine the molecular form of the enzyme, after separation of solubilized membrane proteins on SDS/PAGE and transfer on to nitrocellulose membranes. A single protein band with an apparent molecular mass of 140 kDa was observed. The labelling was abolished by specific neutral endopeptidase inhibitors. This studyprovides the first biochemical characterization of an endopeptidase with catalytic properties similar to those of neutral endopeptidase-24.11 in the mollusc Aplysia californica.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 20:33:48