Determination of the maximum velocity and Michaelis constant of enzymes by a fixed-point method which avoids the necessity to measure initial rates

Duggleby R.G. (1991) Determination of the maximum velocity and Michaelis constant of enzymes by a fixed-point method which avoids the necessity to measure initial rates. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 1078 1: 124-125. doi:10.1016/0167-4838(91)90102-6


Author Duggleby R.G.
Title Determination of the maximum velocity and Michaelis constant of enzymes by a fixed-point method which avoids the necessity to measure initial rates
Journal name Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
ISSN 0167-4838
Publication date 1991-05-30
Sub-type Article (original research)
DOI 10.1016/0167-4838(91)90102-6
Volume 1078
Issue 1
Start page 124
End page 125
Total pages 2
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
1315 Structural Biology
Abstract Measuring the initial velocity is difficult in some enzyme assays where a significant fraction of the substrate is consumed. Here a solution to this problem is proposed; the time to produce a fixed amount of reaction product is measured. This time is inversely proportional to the initial velocity, and is related to the maximum velocity and Michaelis constant by a simple equation and linear plot. The method is illustrated using the reaction catalysed by pyruvate kinase.
Keyword Fixed-point method
Kinetic parameter
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

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