The Purification and Some Properties of H-lysin from Aeromonas salmonicida

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Abstract
H-lysin from A. salmonicida was purified 1770-fold by freeze fractionation, ammonium sulfate 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 hemolysis indicated that the H-lysin had an enzymatic 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 leukocytes, but when it was injected i.v. in rainbow trout no pathological effects were observed.