[Purification of phospholipase C isoenzyme 1 from Clostridium perfringens and its properties].
A procedure for the purification of isoenzyme I of phospholipase C from Cl. perfringens was developed. The isoenzyme was purified to homogeneity (data from disc electrophoresis) using affinity chromatography on polycephamide and gel filtration through Ultrogel AcA-54, the enzyme yield being 41%. Some properties of the purified isoenzyme I (pH and temperature optima, stability, effect of metal ions and detergents, substrate dependence) were investigated. No significant differences between the properties of the unfractionated enzyme and isoenzyme I were established.
Rakhimov
M M
MM
Akhmezhanov
R A
RA
Sof'ina
E Ia
EIa
Sagatova
F A
FA
Shemanova
G F
GF
D002413:Cations, Divalent; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003016:Clostridium perfringens / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D010713:Phosphatidylcholines / Q000378:metabolism; D013501:Surface-Active Agents; D010738:Type C Phospholipases / Q000302:isolation & purification* / Q000378:metabolism
D002413:Cations, Divalent; D007527:Isoenzymes; D010713:Phosphatidylcholines; D013501:Surface-Active Agents; D010738:Type C Phospholipases
Ochistka izofermenta 1 fosfolipazy C iz Clostridium perfringens i nekotorye ego svoĭstva.