Binding properties of Paracentrotus lividus (Echinoidea) hemolysin.
1. Paracentrotus lividus hemolysin binds erythrocytes, zymosan particles, lipopolysaccharide and laminarin surfaces but not auto and allogeneic cell membranes. 2. The binding could, at least for erythrocytes, involve phospholipids and cholesterol. 3. The protease activity of the coelomic fluid is not related to hemolysis. 4. The finding that very low concentrations of Zn2+ inactivate the hemolysin suggests a possible regulative function of the ion in the hemolytic reaction. 5. Ultrastructural observations on rabbit erythrocyte membranes indicate that most likely the transmembrane pores are induced by the lytic molecules.
Department of Biology, University of Lecce, Italy.
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Canicatti
D000818:Animals; D001665:Binding Sites; D004912:Erythrocytes / Q000378:metabolism; D005936:Glucans; D006460:Hemolysin Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008070:Lipopolysaccharides / Q000378:metabolism; D011134:Polysaccharides / Q000378:metabolism; D011817:Rabbits; D012617:Sea Urchins; D015032:Zinc / Q000494:pharmacology; D015054:Zymosan / Q000378:metabolism
D005936:Glucans; D006460:Hemolysin Proteins; D008070:Lipopolysaccharides; D011134:Polysaccharides; C008247:laminaran; D015054:Zymosan; D015032:Zinc