Two-dimensional liquid chromatography study of the human whole saliva proteome.

Autor: Wilmarth PA; 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, Riviere MA, Rustvold DL, Lauten JD, Madden TE, David LL
Jazyk: angličtina
Zdroj: Journal of proteome research [J Proteome Res] 2004 Sep-Oct; Vol. 3 (5), pp. 1017-23.
DOI: 10.1021/pr049911o
Abstrakt: 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.
Databáze: MEDLINE