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Titolo:
DEGRADATION OF VASOACTIVE INTESTINAL POLYPEPTIDE BY RABBIT GASTRIC SMOOTH-MUSCLE MEMBRANES
Autore:
KOBAYASHI R; CHEN YL; LEE TD; DAVIS MT; ITO O; WALSH JH;
Indirizzi:
VET ADM WADSWORTH MED CTR,CTR ULCER RES & EDUC,CTR DIGEST DIS,DEPT MED,BLDG 115 LOS ANGELES CA 90073 VET ADM WADSWORTH MED CTR,CTR ULCER RES & EDUC,CTR DIGEST DIS,DEPT MED,BLDG 115 LOS ANGELES CA 90073 CITY HOPE NATL MED CTR,BECKMAN RES INT DUARTE CA 91010 EISAI CO,RES LABS TSUKUBA 30026 JAPAN
Titolo Testata:
Peptides
fascicolo: 2, volume: 15, anno: 1994,
pagine: 323 - 332
SICI:
0196-9781(1994)15:2<323:DOVIPB>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANGIOTENSIN-CONVERTING ENZYME; MICROSEQUENCE ANALYSIS; NEUTRAL ENDOPEPTIDASE; BIOLOGICAL-ACTIVITIES; EC 3.4.24.11; PEPTIDE VIP; SUBSTANCE-P; CELL-LINE; FRAGMENTS; RELAXATION;
Keywords:
VASOACTIVE INTESTINAL POLYPEPTIDE; RABBIT GASTRIC MUSCLES; MEMBRANE-ASSOCIATED PEPTIDASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
R. Kobayashi et al., "DEGRADATION OF VASOACTIVE INTESTINAL POLYPEPTIDE BY RABBIT GASTRIC SMOOTH-MUSCLE MEMBRANES", Peptides, 15(2), 1994, pp. 323-332

Abstract

Crude membrane fractions prepared from rabbit gastric fundic muscle degraded vasoactive intestinal polypeptide (VIP) with an average specific activity of 0.96 nmol/min/mg protein at 37-degrees-C, pH 7.5, and at [S]0 = 0.05 mM. The relative activities towards [Leu5]enkephalin, substance P, VIP, and neurotensin were approximately 7.7, 2.0, 1.0, and 0.54, respectively. The VIP degradation was inhibited by metal chelators EDTA and o-phenanthroline. CaCl2 at 0.3-1.0 mM enhanced VIP degradation up to twofold. Phosphoramidon, captopril, and bestatin. the specific inhibitors for endopeptidase-24.11, angiotensin-converting enzyme,and aminopeptidase M. respectively, did not affect VIP degradation significantly. However, the complex mixtures of VIP fragments generated implicates action of multiple peptidases including the aforementioned three peptidases and other unidentified peptidase(s).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 08:13:27