Studies on Holothuria polii (Echinodermata) coelomocyte lysate. II. Isolation of coelomocyte hemolysins.
The lytic activity of the Holothuria polii coelomocyte lysate resides in two electrophoretically distinct hemolysins identified as He1 and He2. He1 represents the calcium dependent, heat-labile component whereas He2 is calcium independent and heat-stable. The two hemolysins share serological identity. Both hemolysins appear as single protein molecules of 80KDa molecular weight by SDS-PAGE and transblotting analysis under non-reducing conditions. However under reducing conditions, they are doublets of 76 and 80KDa molecular weight. The hypothesis that the two hemolysins could be isoforms is discussed.
D000818:Animals; D004447:Echinodermata / Q000276:immunology*; D004591:Electrophoresis, Polyacrylamide Gel; D006460:Hemolysin Proteins / Q000276:immunology / Q000302:isolation & purification*; D005779:Immunodiffusion; D008970:Molecular Weight; D012616:Sea Cucumbers / Q000276:immunology*
D006460:Hemolysin Proteins