Australian elapid snakes are amongst the most venomous in the world. Their venoms contain multiple components that target blood hemostasis, neuromuscular signaling, and the cardiovascular system. We describe here a comprehensive approach to separation and identification of the venom proteins from 18 of these snake species, representing 9 genera. The venom protein components were separated by 2D PAGE, and identified using mass spectrometry and de novo peptide sequencing. The venoms are complex mixtures showing up to 200 protein spots varying in size from <7 kDa to over 150 kDa, and in pI from 3 to >10. These include many proteins previously identified in Australian snake venoms, homologs identified in other snake species and some novel proteins. In many cases multiple trains of spots were typically observed in the higher molecular weight range (>20 kDa) (indicative of post-translational modification). Venom proteins and their post-translational modifications were characterised using specific antibodies, phosphoprotein and glycoprotein specific stains, enzymatic digestion, lectin binding and antivenom reactivity. In the lower molecular weight range, several proteins were identified but the predominant species were phospholipase A2 (PLA2) and alpha neurotoxins, both represented by different sequence variants. The higher molecular weight range contained proteases, nucleotidases, oxidases and homologs of mammalian coagulation factors. This information together with the identification of several novel proteins (metalloproteinases, vespryns, PLA2 inhibitors, protein disulfide isomerase, 5` nucleotidases, CRISPs, C-type lectins and acetylcholinesterases) aids in understanding the lethal mechanisms of elapid snake venoms and represents a valuable resource for future development of novel human therapeutics.