Purification and sensitivity of Clostridium chauvoei hemolysin to various erythrocytes.
Using ammonium sulphate fractionation, the Clostridium chauvoei hemolysin was purified by cation exchange chromatography and sephacryl S-100 gel filtration. The molecular mass of the hemolysin, determined by SDS-PAGE was found to be approximately 27kDa. The activity of the hemolysin was determined in erythrocytes of various animals, with sensitivities observed in the order of cow, sheep, chicken, rabbit, rat, mouse, dog and horse. Temperature affected the sensitivity of erythrocytes to C. chauvoei hemolysin. These results may reflect distinct characteristics of the hemolytic activity of C. chauvoei hemolysin and that the hemolysin may be pore-forming.
Mudenda Hang'ombe
Bernard
B
Department of Paraclinical studies, School of Veterinary Medicine, University of Zambia, Lusaka, Zambia. mudenda68@yahoo.com
Kohda
Tomoko
T
Mukamoto
Masafumi
M
Kozaki
Shunji
S
D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D046975:Clostridium chauvoei / Q000737:chemistry* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000187:drug effects* / Q000276:immunology / Q000382:microbiology; D006460:Hemolysin Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D008970:Molecular Weight; D012680:Sensitivity and Specificity
D006460:Hemolysin Proteins