pH-dependence of the phospholipid interaction of diphtheria-toxin fragments.
Photoreactive phospholipids have been used to probe the lipid interaction of diphtheria toxin. Low pH values induce the membrane insertion of both the binding and enzymic fragments of the toxin. The efficiency of this process is much higher with asolectin than with egg lecithin (phosphatidylcholine)/cholesterol liposomes. The low-pH-induced interaction of the toxin fragments with the membrane hydrocarbon phase is more evident for the enzymic A-chain than for the binding B-chain, and it is fully reversed by returning the pH to neutrality.
D004167:Diphtheria Toxin / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008081:Liposomes / Q000378:metabolism; D010713:Phosphatidylcholines; D010743:Phospholipids / Q000378:metabolism*
D004167:Diphtheria Toxin; D008081:Liposomes; D010713:Phosphatidylcholines; D010743:Phospholipids; C037402:1-palmitoyl-2-(2-azido-4-nitro)benzoyl-glycero-3-phosphocholine