Oil bodies, lipid-storage organelles, are stabilized by a number of specific 
proteins. These proteins are very hydrophobic, which complicates their 
identification by "classical" proteomic protocols using trypsin digestion. Due 
to the lack of trypsin cleavage sites, the achievable protein coverage is 
limited or even insufficient for reliable protein identification. To identify 
such proteins and to enhance their coverage, we introduced a modified method 
comprising standard three-step procedure (SDS-PAGE, in-gel digestion, and 
LC-MS/MS analysis). In this method, chymotrypsin, single or in combination with 
trypsin, was used, which enabled to obtain proteolytic peptides from the 
hydrophobic regions and to identify new oil bodies' proteins. Our method can be 
easily applied to identification of other hydrophobic proteins.