Immobilization ofmyo-inositol-1-phosphate synthase containing active, self-regenerating coenzyme (NAD+) on the same matrix
- 20 Downloads
myo-Inositol-1-phosphate synthase (EC 126.96.36.199) from rat testes, an NAD+-containing enzyme, which convertsd-glucose 6-phosphate to 1l-myo-inositol 1-phosphate, could be immobilized together with its cofactor and bovine serum albumin by crosslinking with glutaraldehyde at pH 4.5. The enzyme bound to the gel showed a specific activity of 5.6% of that of the native enzyme, but the activity could be increased to 21% by pretreatment with urea.
Index EntriesGlutaraldehyde crosslinking immobilized inositol phosphate synthase bound NAD synthase immobilized inositol phosphate NAD, immobilization of bound
Unable to display preview. Download preview PDF.
- 1.Davies, P., and Mosbach, K. (1974),Biochim. Biophys. Acta 370, 329–338.Google Scholar
- 2.Wykes, J. R., Dunnill, P., and Lilly, M. D. (1972),Biochim. Biophys. Acta 286, 260–268.Google Scholar
- 5.Malinauskas, A., and Kulys, J. (1978),Prikl. Biokhim. Mikrobiol. 14(6), 919–925.Google Scholar
- 6.Pittner, F., Fried, W., and Hoffmann-Ostenhof, O. (1974),Hoppe Seyler’s Z. Physiol. Chem. 355, 222–224.Google Scholar
- 7.Pittner, F., and Hoffmann-Ostenhof, O. (1979),Molec. Cell. Biochem. 28(1–3), 23–26.Google Scholar
- 8.Barnett, J. E. G., Brice, R. E., and Corina, D. L. (1970),Biochem. J. 119, 183–186.Google Scholar
- 9.Mosbach, K., ed. (1976),Methods Enzymol. 44, 265–268.Google Scholar
- 11.Pittner, F., and Hoffmann-Ostenhof, O. (1978),Hoppe Seyler’s Z. Physiol. Chem. 359, 1395–1400.Google Scholar