Isolation and characterization of the alpha and beta subunits of the platelet-activating glycoprotein from the venom of Crotalus durissus cascavella.
It was concluded in a previous paper that the high Mr platelet-activating glycoprotein isolated earlier from the venom of Crotalus durissus cascavella has an hexameric structure of the alpha 3 beta 3 type involving two distinct subunits. Data reported here demonstrate that these two subunits are separable from each other by ion exchange chromatography under denaturating conditions, have similar Mrs (alpha = 12,540 et beta = 13,770) and exist in a one to one ratio within the native molecule. Carbohydrate analysis indicated that they are both similarly glycosylated to a small extent. They have slightly different amino-acid compositions, a common N-terminal sequence up to the fifth residue and similar extinction coefficients at 280 nm. The native molecule has a calculated Mr of 78,930. Additional data demonstrated that convulxin from the venom of Crotalus durissus terrificus is the same platelet-activating agent as the presently described platelet-activating glycoprotein (PAG) from the venom of Crotalus durissus cascavella.
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D002241:Carbohydrates / Q000032:analysis; D003435:Crotalid Venoms / Q000032:analysis* / Q000302:isolation & purification* / Q000633:toxicity; D006168:Guinea Pigs; D005779:Immunodiffusion; D037181:Lectins, C-Type; D046911:Macromolecular Substances; D008958:Models, Molecular; D008970:Molecular Weight
D000906:Antibodies; D002241:Carbohydrates; D003435:Crotalid Venoms; D037181:Lectins, C-Type; D046911:Macromolecular Substances; C028890:convulxin