Journal ArticleDOI
Coupled enzyme assays: a general expression for the transient.
TLDR
General expressions are presented to describe the transient in a multi-enzyme sequence in which the initial enzyme is rate-limiting, revealing that the initial enzymes does not contribute to the transient but does determine the steady-state velocity.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 1973-02-15. It has received 127 citations till now. The article focuses on the topics: Enzyme assay & Michaelis–Menten kinetics.read more
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Book
The Regulation of Cellular Systems
TL;DR: The basic equations of metabolic control analysis are rewritten in terms of co-response coefficients and internal response coefficients to describe the interaction of optimization methods and the interrelation with evolution.
Journal ArticleDOI
Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases
Hans Merzendorfer,Lars Zimoch +1 more
TL;DR: This review of recent advances in understanding chitin synthesis and its degradation in insects will summarize recent advances.
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Limits of adaptation: the evolution of selective neutrality.
TL;DR: It is proposed that this process is a mechanism whereby conditions for the occurrence of nearly neutral mutations and gene substitutions can be brought about by the long-continued action of natural selection.
References
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Journal ArticleDOI
Biochemical systems analysis. III. Dynamic solutions using a power-law approximation
TL;DR: The approximate dynamic equations are developed in matrix form, and a general program for the solution of an n chemical system using conventional numerical methods is described.
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Kinetic behavior of a two-enzyme membrane carrying out a consecutive set of reactions
TL;DR: The rate of production of the end product at the first stages of the reaction is markedly higher in the immobilized enzyme system than that predicted for a corresponding homogeneous system.
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Human glucose-6-phosphate dehydrogenase: purification of the erythrocyte enzyme and the influence of ions on its activity.
TL;DR: Normal glucose-6-phosphate dehydrogenase from human erythrocytes has been purified 70,000-fold from haemolysates with an overall yield of 30%.