The nature of experimental error in enzyme kinetic measurments
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Analysis of algebraic weighted least-squares estimators for enzyme parametersComprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenaseThe analysis of kinetic data in biochemistry. A critical evaluation of methods.Error structure of enzyme kinetic experiments. Implications for weighting in regression analysis of experimental data.Studies on the mechanism and kinetics of the 2-oxoglutarate dehydrogenase system from pig heart.What happens when data are fitted to the wrong equation?Use of the F test for determining the degree of enzyme-kinetic and ligand-binding data. A Monte Carlo simulation studyFitting of enzyme kinetic data without prior knowledge of weights.Steady-state kinetic studies of the negative co-operativity and flip-flop mechanism for Escherichia coli alkaline phosphatase.Bovine galactosyl transferase. Substrate.managanese complexes and the role of manganese ions in the mechanism.Estimation of the kinetic parameters of undirectional transport across the blood-brain barrier.Comparison of several non-linear-regression methods for fitting the Michaelis-Menten equation.Analytical methods for fitting integrated rate equations. A discontinuous assay.Error structure as a function of substrate and inhibitor concentration in enzyme kinetic experiments.Kinetic evidence for a 'mnemonical' mechanism for rat liver glucokinaseMechanism of regulation of fibroblastic cell replication. IV. An analysis of the serum dependence of cell replication based on Michaelis-Menten kinetics.Application of jackknife procedures to inter-experiment comparisons of parameter estimates for the Michaelis-Menten equation.Optimal observability of sustained stochastic competitive inhibition oscillations at organellar volumes.Kinetics of L-glutamate influx in single barnacle muscle fibers under 0-trans conditions.Thermodynamics of information transfer between subunits in oligomeric enzymes and kinetic cooperativity. 3. Information transfer between the subunits of chloroplast fructose bisphosphatase.
P2860
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P2860
The nature of experimental error in enzyme kinetic measurments
description
1975 nî lūn-bûn
@nan
1975年の論文
@ja
1975年論文
@yue
1975年論文
@zh-hant
1975年論文
@zh-hk
1975年論文
@zh-mo
1975年論文
@zh-tw
1975年论文
@wuu
1975年论文
@zh
1975年论文
@zh-cn
name
The nature of experimental error in enzyme kinetic measurments
@en
type
label
The nature of experimental error in enzyme kinetic measurments
@en
prefLabel
The nature of experimental error in enzyme kinetic measurments
@en
P2093
P2860
P356
P1433
P1476
The nature of experimental error in enzyme kinetic measurments
@en
P2093
Cornish-Bowden A
Darlison MG
P2860
P304
P356
10.1042/BJ1510361
P407
P577
1975-11-01T00:00:00Z