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Mass spectrometry strategies applied to the characterization of proline-rich peptides from secretory parotid granules of pig (Sus scrofa) (Articolo in rivista)

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Mass spectrometry strategies applied to the characterization of proline-rich peptides from secretory parotid granules of pig (Sus scrofa) (Articolo in rivista) (literal)

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Fanali C., Inzitari R., Cabras T., Fiorita A., Scarano E., Patamia M., Petruzzelli R., Bennick A., Messana I., Castagnola M. (2008)
Mass spectrometry strategies applied to the characterization of proline-rich peptides from secretory parotid granules of pig (Sus scrofa)
in Journal of separation science (Print)
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Fanali C., Inzitari R., Cabras T., Fiorita A., Scarano E., Patamia M., Petruzzelli R., Bennick A., Messana I., Castagnola M. (literal)

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Chiara Fanali1 Rosanna Inzitari1 Tiziana Cabras2 Antonella Fiorita3 Emanuele Scarano3 Maria Patamia4 Raffaele Petruzzelli5 Anders Bennick6 Irene Messana2 Massimo Castagnola1, 4 1Institute of Biochemistry and Clinical Biochemistry, Catholic University, Rome, Italy 2Department of Sciences Applied to Biosystems, Cagliari University, Monserrato Campus, Monserrato, Cagliari, Italy 3Institute of Otolaryngology, Catholic University, Rome, Italy 4Institute for the Chemistry of Molecular Recognition, National Research Council (CNR), Rome, Italy 5Department of Biomedical Sciences, University \"G.D'Annunzio\", Chieti Scalo (CH), Italy 6Department of Biochemistry, University of Toronto, Toronto, Canada (literal)

Titolo

Mass spectrometry strategies applied to the characterization of proline-rich peptides from secretory parotid granules of pig (Sus scrofa) (literal)

Abstract

Basic proline-rich proteins (bPRPs) are a class of proteins widely present in saliva of humans and other mammals. They are synthesized as preproproteins and enzymatically cleaved into small peptides before secretion from the salivary glands. Recently, we characterized two proline-rich peptides (SP-A and SP-B) in parotid secretory granules of pig (Sus Scrofa) that are derived from three isoforms of a PRP proprotein (Swiss-Prot data bank: Q95JC9-1, Q95JC9-2 and Q95JC9-3). Together the coding regions for SP-A and SP-B, which are repeated many times, account for 52-70% of the coding regions of the PRP proproteins. This study was undertaken to identify peptides encoded by unassigned regions of the PRP proproteins. RP-HPLC-ESI-IT-MS analysis of enriched granule preparations from pig parotid glands by two different analytical strategies identified ten new proline-rich peptides derived from the three proproteins. Together with the coding regions for SP-A and SP-B already identified it was possible to assign 68-75% of the proproteins coding regions. The peptide sequences indicated a number of unusual proteolytic cleavage sites suggesting the presence of unknown proprotein convertases. (literal)

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