{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T12:06:42Z","timestamp":1789214802828,"version":"build-2803163510"},"reference-count":21,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2008,2,11]],"date-time":"2008-02-11T00:00:00Z","timestamp":1202688000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Separation Science"],"published-print":{"date-parts":[[2008,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Basic proline\u2010rich 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\u2010rich peptides (SP\u2010A and SP\u2010B) in parotid secretory granules of pig (<jats:italic>Sus Scrofa<\/jats:italic>) that are derived from three isoforms of a PRP proprotein (Swiss\u2010Prot data bank:<jats:bold> Q95JC9\u20101<\/jats:bold>, <jats:bold>Q95JC9\u20102 <\/jats:bold>and<jats:bold> Q95JC9\u20103<\/jats:bold>). Together the coding regions for SP\u2010A and SP\u2010B, which are repeated many times, account for 52\u201370% of the coding regions of the PRP proproteins. This study was undertaken to identify peptides encoded by unassigned regions of the PRP proproteins. RP\u2010HPLC\u2010ESI\u2010IT\u2010MS analysis of enriched granule preparations from pig parotid glands by two different analytical strategies identified ten new proline\u2010rich peptides derived from the three proproteins. Together with the coding regions for SP\u2010A and SP\u2010B already identified it was possible to assign 68\u201375% of the proproteins coding regions. The peptide sequences indicated a number of unusual proteolytic cleavage sites suggesting the presence of unknown proprotein convertases.<\/jats:p>","DOI":"10.1002\/jssc.200700343","type":"journal-article","created":{"date-parts":[[2008,2,11]],"date-time":"2008-02-11T16:17:17Z","timestamp":1202746637000},"page":"516-522","source":"Crossref","is-referenced-by-count":10,"title":["Mass spectrometry strategies applied to the characterization of proline\u2010rich peptides from secretory parotid granules of pig (<i>Sus scrofa<\/i>)"],"prefix":"10.1002","volume":"31","author":[{"given":"Chiara","family":"Fanali","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rosanna","family":"Inzitari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tiziana","family":"Cabras","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonella","family":"Fiorita","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emanuele","family":"Scarano","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria","family":"Patamia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Raffaele","family":"Petruzzelli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anders","family":"Bennick","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irene","family":"Messana","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Massimo","family":"Castagnola","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,2,11]]},"reference":[{"key":"e_1_2_1_2_2","first-page":"500","volume":"84","author":"Gorr S. 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