Studies on Holothuria polii (Echinodermata) coelomocyte lysate. I. Hemolytic activity of coelomocyte hemolysins.
The Holothuria polii coelomocyte lysate contains two trypsin-resistant lytic proteins having different chemico-physical properties: a calcium dependent and heat-labile hemolysin that is probably a constitutive component of the coelomic fluid, and another calcium independent and heat-stable one that is released after immunological stimulation; it is therefore not detectable in natural conditions. The sphingomyelin seems to be the membrane receptor with which both hemolysins interact producing lysis.
D000818:Animals; D002122:Calcium Chloride / Q000494:pharmacology; D004447:Echinodermata / Q000502:physiology*; D004492:Edetic Acid / Q000494:pharmacology; D004533:Egtazic Acid / Q000494:pharmacology; D006460:Hemolysin Proteins / Q000302:isolation & purification; D006461:Hemolysis / Q000187:drug effects; D011817:Rabbits; D012756:Sheep; D013109:Sphingomyelins / Q000494:pharmacology; D013696:Temperature
D006460:Hemolysin Proteins; D013109:Sphingomyelins; D004533:Egtazic Acid; D004492:Edetic Acid; D002122:Calcium Chloride