In chromaffin cells taipoxin showed the ability to enter the cells via Ca2+ independent mechanisms. There it enhanced catecholamine release in depolarizing cells by disassembling F-actin in the cytoskeletal barrier. This could lead to a vesicle redistribution promoting immediate access into the subplasmalemmal area. More research studies have found potential binding partners of Taipoxin, which would give more insight into how Taipoxin is transported to the nerve terminals and intramuscular axons. The toxicity of Taipoxin or other PLA2 toxins are often measured with their ability to cut short chain phospholipids or phospholipids-analogues. For Taipoxin PLA2 activity was set on 0.4 mmol/min/mg, and the binding constant (K) of taipoxin would be equal to: KTaipoxin = KA + KB + KC as it consist out of 3 enzymatic domains/subunits. However no correlation was made between PLA2 activity and toxicity, as the pharmacokinetics and the membrane binding properties are more important. A more specific membrane binding would lead to accumulation of taipoxin in the plasma membranes of motor-neurons. The treatment of choice is an antivenom produced by CSL Ltd in 1956 in Australia on the basis of immunised horse plasma. After being bitten the majority of patients will develop systemic envenoming of which clinical evidence is usually present within two hours. This effect can be delayed by applying first aid measures, like immobilization. Additional to neurotoxins taipan venom contains anticoagulants whose effect is also inhibited by the antivenom. Similar to Taipoxin are toxins with different subunits of the PLA domains:  Notexin is a monomer from "Notechis scutatus" venom, β-bungarotoxin is a heterodimer from Chinese banded krait ("Bungarus multicinctus") venom, and textilotoxin is a pentamer from eastern "Pseudonaja textilis" venom.