@article{mbs:/content/journal/micro/10.1099/00221287-131-7-1603, author = "Titball, Richard W. and Munn, Colin B.", title = "The Purification and Some Properties of H-lysin from Aeromonas salmonicida", journal= "Microbiology", year = "1985", volume = "131", number = "7", pages = "1603-1609", doi = "https://doi.org/10.1099/00221287-131-7-1603", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-131-7-1603", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "Summary: 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.", }