[Separation and purification of isoenzymes of Clostridium perfringens phospholipase C].
The procedure for separation and purification of isoenzymes of phospholipase C from Clostridium perfringens (PLC) was developed. The procedure included primary concentration of culture liquid proteins and isoenzyme separtion on DEAE-cellulose during negative sorption of the major isoenzyme. Further purification of the isoenzymes was achieved by (NH4)2SO4 fractionation by Sephadex gel-filtration and isoelectric focusing. During polyacrylamide gel electrophoresis and precipitation reaction in the agar with the antiperfringens hyperimmune serum alpha1-PLC preparations were homogenous. Their coefficient of sedimentation was 3.8 S and isoelectric point was 5.50. The minor isoenzyme alpha2-PLC had the same coefficient of sedimentation and the isoelectric point of 5.35.
D003016:Clostridium perfringens / Q000201:enzymology*; D005779:Immunodiffusion; D007527:Isoenzymes / Q000302:isolation & purification*; D010740:Phospholipases / Q000302:isolation & purification*
D007527:Isoenzymes; D010740:Phospholipases
Razdelenie i ochistka izofermentov fosfolipazy C Clostridium perfringens.