[Preparation of neurotoxin and hemagglutinin from Clostridium botulinum A and characterization of its neurotoxin].
A procedure for preparation of electrophoretically and serologically homogeneous neurotoxin and a highly purified hemagglutinin from the culture fluid of Cl. botulinum A, strain 501 is described. The yield of neurotoxin with specific activity of 80-100 X 10(6) DLM/mg of protein is 5-20%. Neurotoxin has a molecular weight of 150,000, sedimentation coefficient of 7.1S, pI of 6.2-6.3; the maximum of its fluorescence corresponds to 332 nm. The toxin molecule contains 4 SH-groups. Neurotoxin consists of two subunits with molecular weights of 98,000 and 56,000. The storage of neurotoxin at -20 degrees C causes inactivation and electrophoretical heterogeneity of the protein. The inactivation leads to an alteration of the toxin molecule charge, a shift of the lambda max of fluorescence and a loss of the SH-group reactivity without affecting the molecular weight or serological properties of the protein. The data obtained suggest that the conformational state of toxin molecules is essential for its biological activity.
D003014:Clostridium botulinum / Q000032:analysis*; D006388:Hemagglutinins / Q000302:isolation & purification*; D005779:Immunodiffusion; D008970:Molecular Weight; D009498:Neurotoxins / Q000302:isolation & purification* / Q000494:pharmacology; D013050:Spectrometry, Fluorescence; D013438:Sulfhydryl Compounds / Q000032:analysis
D006388:Hemagglutinins; D009498:Neurotoxins; D013438:Sulfhydryl Compounds
Poluchenie neĭrotoksina i gemaggliutinina Clostridium botulinum tipa A i kharakteristika neĭrotoksina.