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Journal ArticleDOI

Kinetic behavior of a two-enzyme membrane carrying out a consecutive set of reactions

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TLDR
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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This article is published in Journal of Theoretical Biology.The article was published on 1971-08-01. It has received 132 citations till now. The article focuses on the topics: Immobilized enzyme & Substrate (chemistry).

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Citations
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Journal ArticleDOI

The immobilization of whole cells: Engineering principles

TL;DR: Techniques which have been used to immobilize whole cells include adsorption, aggregation, confinement and entrapment, and many more have been proposed.
Journal ArticleDOI

Diffusion controlled reaction rates in spheroidal geometry. Application to repressor--operator association and membrane bound enzymes.

TL;DR: The conclusions suggest that the surprisingly high association rate is not essentially due to electrostatic attraction but rather to unspecific binding of represser to nonoperator DNA with subsequent diffusion along the chain.
Journal ArticleDOI

On the role of organized multienzyme systems in cellular metabolism: a general synthesis.

TL;DR: Throughout this article, vector quantities are denoted by use of bold type face and the symbol ▿ denotes the “gradient” operator and δ(r−r′) the three-dimensional Dirac delta function.
Journal ArticleDOI

Prionics or the kinetic basis of prion diseases.

TL;DR: The premise of a linkage between prion aggregation and infection offers a very sensitive method for diagnosing the disease at a very early stage, using fluorescence cross-correlation analysis.
Book ChapterDOI

[29] Kinetic behavior of immobilized enzyme systems

L. Goldstein
TL;DR: This chapter discusses the kinetic behavior of immobilized enzyme systems, which can be controlled by both microenvironmental and mass-transfer effects.
References
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Journal ArticleDOI

A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. Coli I. Purification and characterization of alkaline phosphatase

TL;DR: A procedure for purification of alkaline phosphatase from E. coli is described, and several physical-chemical propetiies of the purified enzyme are reported.
Journal ArticleDOI

The frictional coefficients of the flows of non-electrolytes through artificial membranes.

TL;DR: The phenomenological permeation coefficients were determined for two artificial cellulose membranes of known thickness and water content and it was shown that the geometrical tortuosity does not correspond to a physical Tortuosity.
Journal ArticleDOI

The kinetics of the reaction of nitrophenyl phosphates with alkaline phosphatase from Escherichia coli.

TL;DR: Measurements of the steady-state rate of hydrolysis of 2,4-dinitrophenyl phosphate catalysed by Escherichia coli phosphatase confirmed the above pH-dependence of the ratio of the rates of phosphorylation and dephosphorylation of the enzyme.
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