Relationship between hemagglutinin and sialidase from Clostridium perfringens CN3870: chromatographic characterization of the biologically active proteins.
Biochemical characterization of hemagglutinin and sialidase activities from Clostridium perfringens strain CN3870 revealed that this strain produced three sialidase enzymes that were separable to gel filtration, ion exchange chromatography, and polyacrylamide gel electrophoresis. The molecular weights of sialidase I, II, and III activities were 310,000 +/- 10,000, 105,000 +/- 4,000 and 64,000 +/- 2,000, respectively, the first figure being an approximate value only.
D000373:Agglutinins / Q000032:analysis; D003016:Clostridium perfringens / Q000201:enzymology / Q000276:immunology; D004355:Drug Stability; D004492:Edetic Acid / Q000494:pharmacology; D006388:Hemagglutinins / Q000032:analysis / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000032:analysis / Q000302:isolation & purification; D008970:Molecular Weight; D009154:Mutation; D009439:Neuraminidase / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism; D009532:Nickel / Q000494:pharmacology; D013696:Temperature
D000373:Agglutinins; D006388:Hemagglutinins; D007527:Isoenzymes; D009532:Nickel; D004492:Edetic Acid; D009439:Neuraminidase