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 Mass Spectrometry of glutamine-11 and lysine-29 as acyl donor and acceptor sites

A Malorni;
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.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/142384
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