title: The purification and some properties of H-lysin from Aeromonas salmonicida.
abstract: H-lysin from Aeromonas salmonicida has been purified 1770-fold by freeze fractionation, ammonium sulphate precipitation, ion exchange chromatography and gel filtration chromatography. The purified material was predominantly H-lysin, devoid of detectable T-lysin, caseinase or gelatinase activity, although glycerophospholipid: cholesterol acyltransferase (GCAT) activity was present. The results suggested that H-lysin and GCAT activities were due to different extracellular products. Studies of the kinetics of haemolysis indicated that the H-lysin had an enzymic mode of action, and that initial erythrocyte damage appeared to precede lysis of the cell. The H-lysin was lethal to cultured rainbow trout gonad cells and leucocytes, but when it was injected intravenously in rainbow trout no pathological effects were observed.
mesh_terms: D000333:Aeromonas / Q000032:analysis*; D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004912:Erythrocytes / Q000187:drug effects; D006460:Hemolysin Proteins / Q000302:isolation & purification* / Q000378:metabolism / Q000633:toxicity; D006461:Hemolysis; D007700:Kinetics; D014337:Trout
chemical_list: D006460:Hemolysin Proteins