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Hemolysin of Propionibacterium avidum
Zentralblatt Fur Bakteriologie, Mikrobiologie Und Hygiene. 1. Abt. Originale A, Medizinische Mikrobiologie, Infektionskrankheiten Und Parasitologie = International Journal of Microbiology and Hygiene. A, Medical Microbiology, Infectious
|May 1, 1982
Summary
This study details a thiol-activated hemolysin from Propionibacterium avidum. The hemolysin showed sensitivity to heat, proteases, and deoxyribonuclease, with activity inhibited by copper and lecithin.
Area of Science:
- Microbiology
- Biochemistry
Background:
- Propionibacterium avidum produces extracellular hemolysins.
- Understanding hemolysin properties is crucial for studying bacterial pathogenesis.
Purpose of the Study:
- To partially purify and characterize a thiol-activated extracellular hemolysin from Propionibacterium avidum.
- To investigate the factors affecting hemolysin activity.
Main Methods:
- Partial purification of the hemolysin.
- Assays for heat lability, protease sensitivity, and deoxyribonuclease sensitivity.
- Erythrocyte adsorption studies.
- Inhibition assays using copper ions and lecithin.
Main Results:
- The hemolysin was heat labile and inactivated by proteases and deoxyribonuclease.
- Hemolysin adsorbed to erythrocytes at 0°C.
- Copper ions partially inhibited hemolysis, while lecithin completely prevented it.
- The hemolysin exhibited a broad hemolytic spectrum, with high activity against rabbit, dog, horse, and pig erythrocytes.
Conclusions:
- The characterized hemolysin is a thiol-activated extracellular protein produced by Propionibacterium avidum.
- Its activity is modulated by temperature, enzymes, divalent cations, and lipids.