ADSORPTIVE IMMOBILIZATION OF MICROSOMAL MEMBRANES

Abstract

In this article, the immobilization of microsomal membranes on Fractosil and hexadecylFractosil by hydrophobic adsorption is reported. Microsomes were prepared from rat brain and thecatalytic activity of antimycin A insensitive NADH-cytochrome c reductase (NCCR), one of themembrane bound enzymes in the microsomal electron transport chain, was chosen as a representative ofthe microsomal membrane enzymes. The effect of pH on the enzyme activity and the effect of membraneconcentration on adsorption was explored. Physical adsorption on Fractosil and hexadecyl Fractosilcaused stabilization when the catalytic potential of the enzyme was followed in a continuous operation.The presence of hydrophobic ligand on Fractosil caused higher stabilization of the immobilized enzymeat 25ºC and 4ºC, making it more useful for continuous operations. It is suggested that using supportswith appropriate hydrophobic groups are useful for the immobilization of biologic membranes.