Recent characterization of the whole saliva proteome led to contradictory 
pictures concerning the complexity of its proteome. In this work, 110 proteins 
were analysed by mass spectrometry allowing the identification of 10 accessions 
previously not detected on protein two-dimensional maps, including myosin heavy 
chain (fast skeletal muscle, IIA and IIB), phosphatidylethanolamine binding 
protein, secretory actin-binding protein precursor and triosephosphate 
isomerase. Further comparison with available data demonstrated simultaneously a 
low diversity in terms of variety of accessions and a high complexity in terms 
of number of protein spots identifying the same accession, the two thirds of 
identified spots corresponding to amylases, cystatins and immunoglobulins. This 
diversity may be of interest in the development of non invasive diagnostic tool 
for several disease.