Experimental designs for estimating the parameters of the Michaelis-Menten equation from progress curves of enzyme-catalyzed reactions

Duggleby R.G. and Clarke R.B. (1991) Experimental designs for estimating the parameters of the Michaelis-Menten equation from progress curves of enzyme-catalyzed reactions. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 1080 3: 231-236. doi:10.1016/0167-4838(91)90007-M


Author Duggleby R.G.
Clarke R.B.
Title Experimental designs for estimating the parameters of the Michaelis-Menten equation from progress curves of enzyme-catalyzed reactions
Journal name Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
ISSN 0167-4838
Publication date 1991-11-15
Sub-type Article (original research)
DOI 10.1016/0167-4838(91)90007-M
Volume 1080
Issue 3
Start page 231
End page 236
Total pages 6
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
1315 Structural Biology
Abstract When the progress curve for an enzyme catalyzed reaction follows the integrated Michaelis-Menten equation, the maximum velocity and Michaelis constant can be determined from a single such curve. In this paper, an experimental design for collecting the data is proposed which is close to optimum in the sense that it produces the smallest standard error in the estimate of the Michaelis constant. This design involves choosing an initial substrate concentration which is approx, two or three times the value of the Michaelis constant.
Keyword Enzyme kinetics
Experimental design
Kinetic analysis
Michaelis-Menten kinetics
Progress curve
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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