Two-dimensional liquid chromatography study of the human whole saliva proteome.
The human whole saliva proteome was investigated using two-dimensional liquid chromatography (2-DLC). The 2-DLC study was able to identify, with high confidence, 102 proteins including most known salivary proteins (35), and a large number of common serum proteins (67). Peptides from proline-rich proteins, abundant in saliva, had unusual cleavage sites and were frequently only partially tryptic. Three proteins not previously observed in human saliva were also detected. Significantly greater numbers of identified proteins, including high molecular weight, low molecular weight, and proline-rich proteins, were found with 2-DLC compared to previously reported two-dimensional gel electrophoresis studies.
Department of Integrative Biosciences and Periodontology, School of Dentistry, Oregon Health and Science University, 611 S.W. Campus Drive, Portland, Oregon 97239, USA. wilmarth@ohsu.edu
Phillip A
PA
Wilmarth
Michael A
MA
Riviere
D Leif
DL
Rustvold
Jeffrey D
JD
Lauten
Theresa E
TE
Madden
Larry L
LL
David
D000595:Amino Acid Sequence; D001798:Blood Proteins / Q000032:analysis; D002853:Chromatography, Liquid; D030562:Databases, Protein; D006801:Humans; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D010455:Peptides / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D055232:Proline-Rich Protein Domains; D020543:Proteome / Q000032:analysis* / Q000235:genetics; D012463:Saliva / Q000737:chemistry* / Q000378:metabolism; D012471:Salivary Proteins and Peptides / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D001798:Blood Proteins; D010446:Peptide Fragments; D010455:Peptides; D020543:Proteome; D012471:Salivary Proteins and Peptides; C084798:common salivary protein 1, rat; D014357:Trypsin