Document Type: Regular Paper
1Department of Biochemistry, School of Medicine Shiraz University of Medical Sciences, P. O. Box: 71345-1167, Shiraz, I. R. of Iran
Institute of Biochemistry and Biophysics, University of Tehran, P. O. Box: 13145-1384, Tehran, I. R. of Iran
Department of Biochemistry, School of Medicine Shiraz University of Medical Sciences, P. O. Box: 71345-1167, Shiraz, I. R. of Iran
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 25ºC and 4ºC, 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.