[Proteins from the outer membrane of Pasteurella--1. Polyacrylamide gel electrophoresis of outer membrane proteins--a possibility for differentiation of Pasteurella haemolytica strains].

Using the sodium laurylsarcosinate method, outer membrane proteins (OMPs) of 63 Pasteurella haemolytica strains are isolated and their protein patterns obtained by SDS polyacrylamide gel electrophoresis (SDS-PAGE) are compared. A high degree of similarity became evident both within A and T biotypes in the molecular weight range of 25 to 50 KDa. Strain-to-strain variations are mainly limited to quantitative differences in individual protein bands. It is concluded that within both the A and T biotype groups equal sets of major proteins are present with differing amounts of individual constituents. Biotypes A and T can be clearly distinguished on the basis of marked variations in OMP profiles. OMPs of those AT strains included in comparative studies are exhibiting no general homogeneity, but a relative heterogeneity due to different protein compositions, which are, however, clearly distinct from the patterns of biotypes A and T. It is established unambiguously that isolates belonging to biotypes A or T, as well as AT strains, can be clearly distinguished from each other on the basis of SDS-PAGE analysis of OMP extracts. Thus, polyacrylamide gel electrophoresis of outer membrane proteins can be used for differentiation.