title: Analysis of the lytic activity of the Serpulina hyodysenteriae hemolysin.
abstract: The hemolysins of Serpulina hyodysenteriae are active at 27 to 40 degrees C and pH 3 to 9 and are unaffected by enzymatic inhibitors. Pore formation was demonstrated by the inhibition of hemolysis with molecules of 2.0 to 2.3 nm in diameter and the release of 86rubidium from erythrocytes without hemoglobin release after exposure to native hemolysin.
authors.affiliation: Department of Veterinary Science, The University of Arizona, Tucson 85721, USA. Hyatt@vet.ksu.edu
authors.forename: D R
authors.initials: DR
authors.lastname: Hyatt
authors.forename: L A
authors.initials: LA
authors.lastname: Joens
mesh_terms: D000818:Animals; D017401:Brachyspira hyodysenteriae / Q000472:pathogenicity*; D006460:Hemolysin Proteins / Q000633:toxicity*; D006461:Hemolysis; D011480:Protease Inhibitors / Q000494:pharmacology; D011994:Recombinant Proteins / Q000633:toxicity; D012756:Sheep
chemical_list: D006460:Hemolysin Proteins; D011480:Protease Inhibitors; D011994:Recombinant Proteins