Substance P was found to be an effective acyl donor substrate of transglutaminase in vitro, the reaction products having been examined by both sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fast atom bombardment mass spectrometry. Electrophoretic experiments showed that Substance P incorporated 14C-labeled polyamines when incubated with purified guinea pig liver transglutaminase and Ca2+. Extensive use of fast atom bombardment mass spectrometry allowed to establish that: i) a 1:1 adduct Substance P-spermine is formed; ii) only a single glutamine residue out of two, i.e. Gln-5, acts as acyl donor, iii) the single lysine residue of the neuropeptide is unable to act as acyl acceptor. A direct analytical methodology to detect transglutaminase reaction products is described.
Substance P as a transglutaminase substrate: identification of the reaction products by fast atom bombardment mass spectrometry / Porta, Raffaele; Esposito, C; Metafora, S; Pucci, Pietro; Malorni, A; Marino, Gennaro. - In: ANALYTICAL BIOCHEMISTRY. - ISSN 0003-2697. - STAMPA. - 172:2(1988), pp. 499-503. [10.1016/0003-2697(88)90474-5]
Substance P as a transglutaminase substrate: identification of the reaction products by fast atom bombardment mass spectrometry.
PORTA, RAFFAELE;PUCCI, PIETRO;MARINO, GENNARO
1988
Abstract
Substance P was found to be an effective acyl donor substrate of transglutaminase in vitro, the reaction products having been examined by both sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fast atom bombardment mass spectrometry. Electrophoretic experiments showed that Substance P incorporated 14C-labeled polyamines when incubated with purified guinea pig liver transglutaminase and Ca2+. Extensive use of fast atom bombardment mass spectrometry allowed to establish that: i) a 1:1 adduct Substance P-spermine is formed; ii) only a single glutamine residue out of two, i.e. Gln-5, acts as acyl donor, iii) the single lysine residue of the neuropeptide is unable to act as acyl acceptor. A direct analytical methodology to detect transglutaminase reaction products is described.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.