Purification and partial characterization of a cohaemolysin (CAMP-factor) produced by Streptococcus canis.
A cohaemolysin from the culture supernate of a canine pathogenic group G streptococcus (S. canis) was purified to electrophoretic homogeneity. The purification procedure involved ammonium sulphate precipitation, ultrafiltration, gel filtration and preparative isoelectric focusing. The cohaemolysin consisted of a single polypeptide chain, 18.6 kDa, with an isoelectric point at pH 5.1. The protein reacted with an homologous antiserum, appeared to be trypsin-sensitive and relatively heat-stable. The cohaemolysin did not show any non-specific IgG binding activities.
Gürtürk
K
K
Institut für Bakteriologie und Immunologie, Justus-Liebig-Universität, Giessen, F.R.G.
Lämmler
C
C
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D004285:Dogs / Q000382:microbiology; D006460:Hemolysin Proteins / Q000737:chemistry / Q000302:isolation & purification*; D008970:Molecular Weight; D013291:Streptococcus / Q000032:analysis*
D001426:Bacterial Proteins; C039092:CAMP protein, Streptococcus; D006460:Hemolysin Proteins