Purification and partial characterization of a cohaemolysin (CAMP-factor) produced by Streptococcus canis.
نویسندگان
چکیده
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.
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ورودعنوان ژورنال:
- FEMS microbiology immunology
دوره 2 2 شماره
صفحات -
تاریخ انتشار 1990