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Titolo:
Expression of the acidic stretch of nardilysin as a functional binding domain
Autore:
Ma, ZL; Csuhai, E; Chow, KM; Hersh, LB;
Indirizzi:
Univ Kentucky, Albert B Chandler Med Ctr, Dept Mol & Cellular Biochem, Lexington, KY 40536 USA Univ Kentucky Lexington KY USA 40536 lar Biochem, Lexington, KY 40536 USA Transylvania Univ, Dept Chem, Lexington, KY 40508 USA Transylvania Univ Lexington KY USA 40508 pt Chem, Lexington, KY 40508 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 31, volume: 40, anno: 2001,
pagine: 9447 - 9452
SICI:
0006-2960(20010807)40:31<9447:EOTASO>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARGININE DIBASIC CONVERTASE; NRD CONVERTASE; METALLOENDOPEPTIDASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
13
Recensione:
Indirizzi per estratti:
Indirizzo: Hersh, LB Univ Kentucky, Albert B Chandler Med Ctr, Dept Mol & Cellular Biochem, 800Rose St, Lexington, KY 40536 USA Univ Kentucky 800 Rose St Lexington KY USA 40536 n, KY 40536 USA
Citazione:
Z.L. Ma et al., "Expression of the acidic stretch of nardilysin as a functional binding domain", BIOCHEM, 40(31), 2001, pp. 9447-9452

Abstract

Kinetic evidence suggests an acidic region in nardilysin binds polyamines and acts as a regulatory domain. The binding of similar to5 mol of spermine/mol of nardilysin was demonstrated. The binding curve was sigmoidal exhibiting an IC50 of similar to 118 muM and a Hill coefficient of 1.8. Spermine diminished the tryptophan fluorescence of the enzyme and increased its sensitivity to protease V8. The acidic stretch from mouse and human nardilysin were expressed as glutathione transferase fusion proteins. All fusion proteins bound spermine with an IC50 of 40 to 110 muM. The mouse fusion protein bound similar to7 mol of spermine exhibiting a sigmoidal binding curve and a Hill coefficient of 1.4. The human acidic stretch, containing fewer acidic residues, bound similar to5 mol of spermine/mol with a hyperbolic bindingcurve. Chimeric fusion proteins containing the N-terminus of the mouse acidic region fused to the C-terminus of the human acidic region bound similarto 10 mol of spermine, while the opposite chimera bound similar to4 mol ofspermine/mol. The N-terminal region of the mouse acidic domain binds 3-4 mol spermine/mol exhibiting a Hill coefficient of 1.4, while the same regionfrom human nardilysin binds 1 mol of spermine/mol. Spermine enhanced the sensitivity of the mouse acidic domain, but not the human acidic domain, to protease V8. Together the data support a model where the acidic stretch of nardilysin functions as an autonomous domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 18:14:53