Isolation of the major outer-membrane protein of Actinobacillus pleuropneumoniae and Haemophilus parasuis.
A polyclonal antibody against the 35 kDa major outer-membrane protein of Pasteurella multocida cross-reacted with the 40 kDa major outer-membrane protein of Actinobacillus pleuropneumoniae and the 42 kDa major outer-membrane protein of Haemophilus parasuis. The N-terminal amino-acid sequences of these proteins revealed a strong homology with the putative 35 kDa porin protein of Pasteurella multocida (66.7 and 76.2%, respectively). Significant homologies were also evident between the 40 kDa and the 42 kDa protein (76.2%), and with non-specific porins of gram-negative bacteria.
D016977:Actinobacillus pleuropneumoniae / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification*; D006190:Haemophilus / Q000737:chemistry*; D008969:Molecular Sequence Data; D016979:Pasteurella multocida / Q000737:chemistry; D016415:Sequence Alignment / Q000662:veterinary; D017386:Sequence Homology, Amino Acid; D013552:Swine
D001425:Bacterial Outer Membrane Proteins