Assessment of a complex mixture of interacting proteins in the coagulant active venom from Agkistrodon contortrix contortrix.

The crude venom of Agkistrodon contortrix contortrix was characterized by means of 2D-PAGE (using various separation principles in the respective directions) and high performance gel filtration chromatography. It was found that the venom presents a rich and remarkably stable mixture of proteins, mostly glycoproteins, which may interact each other. High stability of the venom in spite of the presence of many proteolytic enzymes, must most likely be attributed to the sugar moieties of venom proteins. Carbohydrate composition also causes considerable heterogeneity in charge and the presence of wide range of charge isomers. The intricate complexity of the venom makes it a real difficult-to-separate mixture.