Preparation of Antibody-Coupled Liposomes Containing Horseradish Peroxidase as a Marker Molecule
Horseradish peroxidase (HRP) was encapsulated in liposomes prepared by an extrusion technique. The liposomes were coupled covalently to anti-rabbit IgG using N-hydroxysuccinimide ester palmitic acid as a component of liposomes. The number of encapsulated HRP molecules per liposome was about 800. A large portion of HRP was encapsulated inside the liposomes for about one week at 4°C. The catalytic activity of HRP was measured by a luminol chemiluminescence (CL) method and was found to be almost constant during storage. The CL intensity per antibody in the detection of HRP encapsulated in the antibody-coupled liposomes was 125-times greater than that of HRP conjugated directly to the antibody.
- Analytical sciences : the international journal of the Japan Society for Analytical Chemistry
Analytical sciences : the international journal of the Japan Society for Analytical Chemistry 15(4), 349-352, 1999-04