OBJECTIVESTo evaluate the application of two-dimensional electrophoresis and mass spectrometry in the research of proteins expressed in testis.

METHODSProtein from adult ICR mouse testes was extracted by two-dimensional electrophoresis. Two protein spots were cut from the gel, then the proteins were digested in-gel by enzyme and the generated peptides were measured by matrix assisted laser desorption/ionization-time of flight mass spectrometry. The proteins were identified through database searching.

RESULTSTwo spots in Commasie Brilliant Blue-stained gel were identified as serum albumin and protein disulfide isomerase by database searching.

CONCLUSIONSThis rapid high resolution and efficient method is a very powerful way to analyze testicular proteins.