The nature of the random experimental error encountered when acetylcholine hydrolase and alcohol dehydrogenase are assayed
- 1 April 1979
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 94 (2) , 265-269
- https://doi.org/10.1016/0003-2697(79)90358-0
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- A nonparametric method for fitting a single exponential to biological dataAnalytical Biochemistry, 1979
- An Evaluation of Methods for Determining the Initial Velocities of Enzyme-Catalysed Reactions from Progress CurvesBiochemical Society Transactions, 1978
- An Evaluation of Three Methods for Fitting the Michaelis-Menten Equation to Sets of Data with a Common Michaelis Constant but Different Maximum VelocitiesBiochemical Society Transactions, 1978
- The Nature of the Random Experimental Error Encountered when the Kinetics of Acetylcholine Hydrolase are DeterminedBiochemical Society Transactions, 1977
- The Kinetics of Human Erythrocyte Acetylcholine Hydrolase before and after Solubilization with Triton X-100Biochemical Society Transactions, 1976
- Error Structure of Enzyme Kinetic Experiments. Implications for Weighting in Regression Analysis of Experimental DataEuropean Journal of Biochemistry, 1976
- The nature of experimental error in enzyme kinetic measurmentsBiochemical Journal, 1975
- A comparison of seven methods for fitting the Michaelis-Menten equationBiochemical Journal, 1975
- A computer program for fitting and statistically analyzing initial rate data applied to bovine hexokinase type III isozymeArchives of Biochemistry and Biophysics, 1975
- The direct linear plot. A new graphical procedure for estimating enzyme kinetic parametersBiochemical Journal, 1974