Statistical Calculations of the Accuracy of the Michaelis Constant from Viscosimetric Determinations of Polymetaphosphatase and Dextranase Activity.
- 1 January 1967
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 21 (6) , 1575-1580
- https://doi.org/10.3891/acta.chem.scand.21-1575
Abstract
Values for Michaelis'' constant obtained with different preparations of polymeric homologous substrates can be compared by standard statistical methods if the accuracy is known, but the most common procedures for the calculation of Michaelis'' constant are not suitable for statistical accuracy calculations according to the method of least squares; however, Hanes'' equation [S]/v = Km/V + (1/V)-[S] is suitable. The use of this equation for accuracy calculations is exemplified. For Aspergillus niger polymetaphosphatase the values of Michaelis'' constant showed no significant difference for 3 preparations of polymetaphosphate, whereas a 4th preparation with a larger fraction of low molecular weight substance gave a deviating result. The 80% confidence interval for the weighted mean value of the Michaelis'' constant for the 3 preparations was 0.06-0.13% at 25[degree]C and pH 5.4 in acetate buffer of the ionic strength 0.3. For Cellvibrio fulva dextranase the 95% confidence interval for a determination of the Michaelis'' constant was 0.1-0.6% at 25[degree]C and pH 5.22; the 50% confidence interval was 0.31-0.40%.This publication has 4 references indexed in Scilit:
- Viscosimetric Determination of Cellulase Activity in the Intestine of the Sea Urchin: Reaction Mechanism and Equilibrium Constant for Cellulase Stabilization with Calcium.Acta Chemica Scandinavica, 1966
- Statistical estimations in enzyme kineticsBiochemical Journal, 1961
- Investigations on Dextranase. I. On the Occurrence and the Assay of Dextranase.Acta Chemica Scandinavica, 1949
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934