The Preparation and Kinetics of Lactate Dehydrogenase Attached to Water-insoluble Particles and Sheets

Overview

Journal Biochem J

Specialty Biochemistry

Date 1968 Aug 1

PMID 5673529

Citations 4

Authors

R J Wilson

G Kay

M D Lilly

Affiliations

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Abstract

1. The preparation of lactate dehydrogenase covalently attached to anion-exchange cellulose particles and sheets by use of a dichloro-sym-triazinyl dyestuff, Procion brilliant orange MGS, is described. 2. The stability and kinetic properties of these preparations were investigated. 3. An equation is derived to describe the change in concentration of a substrate when passed through a uniform bed of a substrate-inhibited enzyme. A number of theoretical curves are shown to illustrate the system. 4. A titrimetric assay for lactate dehydrogenase is described, and shown to be stoicheiometric over the range pH5.0-9.2. 5. The results are discussed in relation to previous work, and the effects of charged groups on the support, and of the diffusion film surrounding any particle in suspension, are treated qualitatively.

Citing Articles

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Green M, CRUTCHFIELD G Biochem J. 1969; 115(2):183-90.

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Diffusional increase and decrease in half-maximal-activity substrate concentrations with two-substrate enzymic reactions.

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