Structural characterization of a new statherin from pig parotid granules (pages 269–275)
Barbara Manconi, Chiara Fanali, Tiziana Cabras, Rosanna Inzitari, Maria Patamia, Emanuele Scarano, Antonella Fiorita, Alberto Vitali, Massimo Castagnola, Irene Messana and Maria Teresa Sanna
Version of Record online: 7 MAY 2010 | DOI: 10.1002/psc.1232
HPLC– ESI-MS analysis on pig parotid secretory granule extracts evidenced a peptide with a molecular mass value of 5381.1 ± 0.6 Da and its truncated form, devoid of the C-terminal Ala, with typical structural features of the four statherins characterized till now. Pig statherin is mono-phoshorylated on Ser-3, while primate statherins already characterized are di-phosphorylated on Ser-2 and Ser-3. This difference, probably, connected to the Asp-4 Glu substitution, suggests the involvement of the Golgi-casein kinase, which strictly recognizes the SX(E/pS) consensus sequence.