Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
STRUCTURAL ROLE OF DISULFIDE BRIDGES IN THE CYCLIC ADP-RIBOSE RELATEDBIFUNCTIONAL ECTOENZYME CD38
Autore:
GUIDA L; FRANCO L; ZOCCHI E; DEFLORA A;
Indirizzi:
UNIV GENOA,INST BIOCHEM,VIALE BENEDETTO XVI1 I-16132 GENOA ITALY UNIV GENOA,INST BIOCHEM I-16132 GENOA ITALY ADV BIOTECHNOL CTR I-16132 GENOA ITALY
Titolo Testata:
FEBS letters
fascicolo: 3, volume: 368, anno: 1995,
pagine: 481 - 484
SICI:
0014-5793(1995)368:3<481:SRODBI>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
LYMPHOCYTE ANTIGEN CD38; HUMAN ERYTHROCYTES; OUTER SURFACE; HYDROLYSIS; CYCLASE; GLYCOHYDROLASE; MOLECULE; ACID; NAD+;
Keywords:
CD38; HUMAN ERYTHROCYTE; ADP-RIBOSYL CYCLASE; CYCLIC ADP-RIBOSE HYDROLASE; DISULFIDE BOND; APLYSIA CALIFORNICA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
L. Guida et al., "STRUCTURAL ROLE OF DISULFIDE BRIDGES IN THE CYCLIC ADP-RIBOSE RELATEDBIFUNCTIONAL ECTOENZYME CD38", FEBS letters, 368(3), 1995, pp. 481-484

Abstract

Human CD38, a type II cell surface glycoprotein, is a bifunctional ectoenzyme catalyzing both ADP-ribosyl cyclase and cyclic ADP-ribose (cADPR) hydrolase reactions. It shares a high degree of sequence homologywith the cyclase from Aplysia species and studies of site-directed mutagenesis have recently demonstrated the importance, but not elucidated the role, of several cysteine residues highly conserved between these proteins, N-Ethylmaleimide, iodoacetamide and thiol-oxidizing reagents failed to affect either the cyclase or the weaker hydrolase activity of the Aplysia califor nica protein. Likewise, these reagents did not impair the two activities of CD38 purified from human erythrocytes. beta-mercaptoethanol had no effect on the Aplysia enzyme activities, while it inactivated both the cyclase and the cADPR hydrolase of CD38 by inducing its extensive oligomerization. In intact erythrocytes the beta-mercaptoethanol-dependent enzyme inactivation was completely prevented by prior cross-linking of the membrane proteins with glutaraldehyde. These data demonstrate that none of the cysteine residues plays any direct catalytic role in CD38 and Aplysia proteins, and that disulfide bridges are essential for maintaining the monomeric, catalytically active structure of CD38.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 18:54:01