Characterization and comparison of soluble and immobilized pig muscle aldolases
- 35 Downloads
Pig muscle aldolase was insolubilized by covalent attachment to a polyacrylamide matrix containing carboxylic functional groups. The catalytic activity of the Akrilex C-aldolase was 2014 units/g solid, i.e., an activity loss of only about 5% relative to the initial activity. The pH optimum for catalytic activity shifted form 7.25 to 7.5 and the apparent temperature optimum from 313 to 318 K. The Michaelis constant of the insolubilized enzyme was significantly higher than that of the soluble aldolase. Heat- and urea-inactivation experiments revealed that the immobilization increased the stability of the enzyme.
Index EntriesImmobilized aldolase pig muscle aldolase covalent attachment polyacrylamide matrix, containing carboxylic functional groups Akrilex C-100 gel, with high aldolase activity aldolase, with high stability
Unable to display preview. Download preview PDF.
- 3.Marshall, D. J. (1974), inImmobilized Biochemicals and Affinity Chromatography, Dunlap, R. B., ed., Plenum, New York, pp. 354–356.Google Scholar
- 7.Schell, H. D., Scholnic, L., and Carstenau, M. (1977),Stud. Cercet. Biochim. 20, 77.Google Scholar
- 9.Ábrahám, M., Horváth, L., and Szajáni, B. (1985), Comp. Biochem. Physiol, in press.Google Scholar
- 10.Szajáni, B., Ivony, K., and Boross, L. (1980),Acta Biochim. Biophys. Acad. Sci. Hung. 15, 295.Google Scholar
- 11.Szajáni, B., Ivony, K., and Boross, L. (1980),J. Appl. Biochem. 2, 72.Google Scholar
- 12.Kovács, K., Szajáni, B., and Boross, L. (1980),J. Appl. Biochem. 4, 11.Google Scholar
- 13.Lowry, O. H., Rosebrough, N. J., Farr, L., and Randall, R. J. (1951),J. Biol. Chem. 193, 503.Google Scholar
- 14.Sibley, J. A., and Lehninger, A. L. (1948),J. Biol. Chem. 177, 859.Google Scholar