The purpose of the study was both to estimate the electrophoretic profiles (SDS-PAGE) of outer membrane proteins among Salmonella Enteritidis strains isolated from humans and poultry, as well as to identify the antigens which can induce the appearance of a specific antibody response among vaccinated animals. The densitometry analysis of electrophoregrams showed that a single protein complex of 21 fractions was distinctive for strains grown in standard conditions. Among these fractions those with 20, 22, 35 and 37 kDa characterized by high optical density were found dominant. A single protein profile with 24 fractions was also characteristic of strains grown in conditions with restricted access to iron ions. A high optical density was a feature of proteins with 19, 35, 37, 55 and 74 kDa. Adding of 200 µM 2,2’-dipirydyl to the culture medium caused the expression of proteins and 78 kDa taking part in obtaining and transporting iron through S. Enteritidis within a mass range of 19, 55, 70, and 74. Densitometry analysis of electrophoregrams obtained from nitrocellulose membranes for proteins from bacterial strains grown in conditions with restricted access to iron ions indicated the presence of specific, intensive reactions towards the antigens of 35 and 55 kDa. As far as proteins obtained from bacterial culture grown with and without the addition of chelator were concerned, distinctive reactions were found towards antigens of 35 and 58 kDa. The main protein present in electrophoregrams of bacteria grown both with and without a supplement of chelator and in immunoblotting reactions was that of 35 kDa, belonging to porins of OmpA type.