[Investigation of outer membrane proteins of Pasteurella. 2: Iron-regulated outer membrane proteins of Pasteurella multocida and Pasteurella haemolytica]. / Untersuchungen zu den Proteinen der äusseren Membran von Pasteurellen 2. Mitteilung: Eisenregulierte Proteine der äusseren Membran bei Pasteurella multocida und Pasteurella haemolytica.

Pasteurella multocida and Pasteurella haemolytica produce specific proteins in the outer membrane under iron-depleted conditions. Pasteurella multocida serovar A expresses these proteins of molecular masses of 76 and 96 kDa as determined by electrophoresis. The analogous serovar D produces a further iron-regulated protein of 85 kDa. The Pasteurella haemolytica strains of serovar A1, A6 and T contain iron-regulated outer membrane proteins of molecular masses of 71, 77 and 100 kDa. These proteins possess binding positions for iron ions. Both Pasteurella multocida and Pasteurella haemolytica strains utilize iron from porcine and bovine transferrin, but not from haemin and haemoglobin.

[Proteins from the outer membrane of Pasteurella--1. Polyacrylamide gel electrophoresis of outer membrane proteins--a possibility for differentiation of Pasteurella haemolytica strains]. / Untersuchungen zu den Proteinen der äusseren Membran von Pasteurellen--1. Mitteilung: Polyacrylamidgelelektrophorese von Proteinen der äusseren Membran--eine Möglichkeit der Differenzierung von Pasteurella-haemolytica-Stämmen.

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.