Analytical Sciences

Preparation of Antibody-Coupled Liposomes Containing Horseradish Peroxidase as a Marker Molecule

Takahiro SUITA and Tamio KAMIDATE *

Graduate School of Engineering, Hokkaido University, Sapporo 060-8628, Japan

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 4ûÃ. 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. (Keywords: Liposome, horseradish peroxidase, luminol, chemiluminescence)

J-STAGE: View this article in J-STAGE