Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Identical primary sequence but different conformations of the bioactive regions of canine CCK-8 and CCK-58
Autore:
Keire, DA; Solomon, TE; Reeve, JR;
Indirizzi:
Greater Los Angeles Vet Hlth Care Syst, CURE, Digest Dis Res Ctr, Los Angeles, CA 90073 USA Greater Los Angeles Vet Hlth Care Syst Los Angeles CA USA 90073 90073 USA Univ Calif Los Angeles, Sch Med, Div Digest Dis, Los Angeles, CA 90023 USAUniv Calif Los Angeles Los Angeles CA USA 90023 Los Angeles, CA 90023 USA
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 2, volume: 266, anno: 1999,
pagine: 400 - 404
SICI:
0006-291X(199912)266:2<400:IPSBDC>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
FLUORESCENCE-TRANSFER MEASUREMENTS; H-1-NMR SPECTROSCOPY; CHOLECYSTOKININ; FRAGMENTS; BRAIN; BLOOD;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Reeve, JR Greater Los Angeles Vet Hlth Care Syst, CURE, Digest Dis Res Ctr, Room 115,Bldg 115, Los Angeles, CA 90073 USA Greater Los Angeles Vet HlthCare Syst Room 115,Bldg 115 Los Angeles CA USA 90073
Citazione:
D.A. Keire et al., "Identical primary sequence but different conformations of the bioactive regions of canine CCK-8 and CCK-58", BIOC BIOP R, 266(2), 1999, pp. 400-404

Abstract

The C-terminal bioactive regions of CCK-8 and CCK-58 are identical (DY*MGWMDF-NH2, Y* denotes a sulfated tyrosine residue), but these peptides have different patterns of bioactivity. Specifically, CCK-58 binds more avidly tothe CCKA receptor while CCK-8 is more potent for stimulation of amylase secretion from pancreatic acini. We postulate that these seemingly contradictory observations reflect a stable conformational change in CCK-58 that enhances binding, but diminishes activation of second messenger. We used CD andNMR spectra to evaluate postulated structural differences between CCK-8 and the carboxy-terminus of synthetic CCK-58. The CD spectra indicate the presence of turns in CCK-8 but a mixture of helical and random coil structuresfor CCK-58. Comparisons of partial NMR chemical shift assignments of CCK-58 and full assignments for CCK-8 also indicate differences in the backbone conformations for these residues. The data support the hypothesis that these peptides have different, stable, carboxy-terminal structures that may influence bioactivity. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 06:09:06