I--isolation and electron microscope studies of a potent platelet-aggregating glycoprotein from the venom of Crotalus durissus cascavella.
A potent acid-soluble platelet-aggregating glycoprotein was purified from the venom of Crotalus durissus cascavella by molecular sieve chromatography on Sephadex G-75 and by adsorption onto Sepharose 4B gels at acidic pH. This new protein with an apparent Mr of 300,000 at acidic pH and containing a low amount of sugars is non-toxic for mice. Electron microscope studies showed that the platelet-aggregating glycoprotein appeared as regular rosettes of 150 A in diameter at acidic pH and underwent polymerization in rod-like particles in the presence of sodium chloride. This glycoprotein, probably hydrophobic, is dissociated into an active molecular form whose apparent Mr was 144,000; however, it is believed to still be a not totally dissociated molecule.
D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D003435:Crotalid Venoms / Q000032:analysis*; D004950:Esterases; D006023:Glycoproteins / Q000032:analysis*; D066298:In Vitro Techniques; D037181:Lectins, C-Type; D008854:Microscopy, Electron; D010741:Phospholipases A / Q000378:metabolism; D010974:Platelet Aggregation / Q000187:drug effects*; D011487:Protein Conformation; D011817:Rabbits
D002241:Carbohydrates; D003435:Crotalid Venoms; D006023:Glycoproteins; D037181:Lectins, C-Type; C028890:convulxin; D004950:Esterases; D010741:Phospholipases A