Comparative study of horseradish peroxidase immobilization on modification of a gold surface using a surface plasmon resonance method

Horseradish peroxidase is immobilized by a periodate method on the gold surfaces previously modified with 16-mercapto-hexadecanoic acid or with hydrogen disulfide and soybean trypsin inhibitor. The effect of gold surface modification conditions on the immobilization of the enzyme as well as on the properties of the immobilized glycoprotein are studied using surface plasmon resonance technique. Restoration of the ability to bind specific antibodies is demonstrated for the immobilized enzyme. The low level of non-specific antibody binding to the immobilized glycoprotein is also shown.