title: Studies on Holothuria polii (Echinodermata) coelomocyte lysate. II. Isolation of coelomocyte hemolysins.
abstract: 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.
mesh_terms: 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*
chemical_list: D006460:Hemolysin Proteins