چكيده لاتين :
In this article, the immobilization of microsomal membranes on Fractosil and hexadecyl Fractosil by hydrophobic adsorption is reported. Microsomes were prepared from rat brain and the catalytic activity of antimycin A insensitive NADH-cytochrome c reductase (NCCR), one of the membrane bound enzymes in the microsomal electron transport chain, was chosen as a representative of the microsomal membrane enzymes. The effect of pH on the enzyme activity and the effect of membrane concentration on adsorption was explored. Physical adsorption on Fractosil and hexadecyl Fractosil caused 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 enzyme at 25?C and 4?C, making it more useful for continuous operations. It is suggested that using supports with appropriate hydrophobic groups are useful for the immobilization of biologic membranes.
