FAB-Mapping strategy was successfully exploited to characterize the reaction products of the transglutaminase-mediated modifications of human beta-endorphin in vitro. The GLN-11 residue of the neuropeptide was shown to be an effective acyl donor site for the enzyme, being able to bind spermine in the presence of Ca2+. Moreover, only one out of five lysyl residues (LYS-29) was demonstrated to act as acyl acceptor crosslinking with GLN-11.
Beta-endorphin modification by transglutaminase in vitro: identification by FAB/MS of glutamine-11 and lysine-29 as acyl donor and acceptor sites / Pucci, P., Malorni, A., Marino, G., Metafora, S., Esposito, C., Porta, R.. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - STAMPA. - 154:2(1988), pp. 735-740. [10.1016/0006-291X(88)90201-X]
Beta-endorphin modification by transglutaminase in vitro: identification by FAB/MS of glutamine-11 and lysine-29 as acyl donor and acceptor sites.
PUCCI, PIETRO;MARINO, GENNARO;PORTA, RAFFAELE
1988
Abstract
FAB-Mapping strategy was successfully exploited to characterize the reaction products of the transglutaminase-mediated modifications of human beta-endorphin in vitro. The GLN-11 residue of the neuropeptide was shown to be an effective acyl donor site for the enzyme, being able to bind spermine in the presence of Ca2+. Moreover, only one out of five lysyl residues (LYS-29) was demonstrated to act as acyl acceptor crosslinking with GLN-11.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
