[Use of phosphatidylinositol as a hydrophobic anchor for protein binding with liposomes]

For binding of proteins with the membranes of liposomes, natural lipid phosphatidylinozite was proposed. First, it was activated by periodate, then in incubation with protein in alkaline medium the binding between the modifier and the protein was covalent. Liposomes with the bound protein are obtained by dialysis detergent removal. In binding of the pattern protein alpha-chymotripsin with liposomes from egg phosphatidylcholine there was reached the binding of 2,4 . 10(-3) M of protein per mole of the lipid. 70% of the enzyme immobilized on liposomes was observed to completely retain its affinity to pancreatic tripsin inhibitor. Thermostability of the immobilized enzyme was studied.