Hemolysin of Propionibacterium avidum.
Thiol-activated extracellular hemolysin produced by a strain of Propionibacterium avidum was partially purified and several properties were examined. The hemolysin was heat labile and inactivated by proteases and deoxyribonuclease. Hemolysin adsorbed to erythrocytes at 0 degrees C. Cu++ at 1 mM inhibited hemolysis partially. Lecithin prevented the activity completely. The hemolytic spectrum was relatively wide and the activity was high with rabbit, dog, horse, and pig erythrocytes.
D000818:Animals; D002413:Cations, Divalent / Q000494:pharmacology; D003851:Deoxyribonucleases / Q000494:pharmacology; D004285:Dogs; D006460:Hemolysin Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D006461:Hemolysis; D006736:Horses; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000494:pharmacology; D011424:Propionibacterium / Q000032:analysis*; D011817:Rabbits; D013552:Swine; D013696:Temperature
D002413:Cations, Divalent; D006460:Hemolysin Proteins; D003851:Deoxyribonucleases; D010447:Peptide Hydrolases