Benvenuti nell'Anagrafe della Ricerca d'Ateneo
La valutazione delle attività di ricerca che si svolgono nelle università ha assunto un'importanza rilevante sia per l'intero sistema universitario sia all'interno di ogni singolo ateneo. Roma Tre si è quindi dotata di idonei strumenti informativi in grado di supportare al meglio le azioni di monitoraggio e di valutazione delle attività di ricerca svolte nei propri dipartimentied ha realizzato una Anagrafe della Ricerca di Ateneo.
EnglishHuman serum albumin (HSA) displays esterase activity reflecting multiple irreversible chemical modifications rather than turnover. Here, kinetics of the pseudo-enzymatic hydrolysis of 4-nitrophenyl acetate (NphOAc) are reported. Under conditions where [HSA] >= 5x [NphOAc] and [NphOAc] 5x [HSA], the HSA-catalyzed hydrolysis of NphOAc is a first-order process for more than 95% of its course. From the dependence of the apparent rate constants k(app) and k(obs) on [HSA] and [NphOAc], respectively, values of K-s, k(+2), and k(+2)/K-s were determined. Values of K-s, k(+2), and k(+2/K), obtained at [HSA] 5 x [NphOAc] and [NphOAc],>= 5 x [HSA] are in good agreement, the deacylation step being rate limiting in catalysis. The pH-dependence of k(+2)/K-s, k(+2), and K, reflects the acidic pK(a) shift of the Tyr411 catalytic residue from 9.0 +/- 0.1 in the substrate-free HSA to 8.1 +/- 0.1 in the HSA:NphOAc complex. Accordingly, diazepam inhibits competitively the HSA-catalyzed hydrolysis of NphOAc by binding to Tyr411
Ascenzi P, Gioia M, Fanali G, Coletta M, & Fasano M (2012). Pseudo-enzymatic hydrolysis of 4-nitrophenyl acetate by human serum albumin: pH-dependence of rates of individual steps. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 424(3), 451-455.
| Titolo: | Pseudo-enzymatic hydrolysis of 4-nitrophenyl acetate by human serum albumin: pH-dependence of rates of individual steps | |
| Autori: | ||
| Data di pubblicazione: | 2012 | |
| Rivista: | ||
| Citazione: | Ascenzi P, Gioia M, Fanali G, Coletta M, & Fasano M (2012). Pseudo-enzymatic hydrolysis of 4-nitrophenyl acetate by human serum albumin: pH-dependence of rates of individual steps. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 424(3), 451-455. | |
| Handle: | http://hdl.handle.net/11590/136896 | |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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