Aug 25, 1976

Quantitative cytochemical measurement of glyceraldehyde 3-phosphate dehydrogenase activity

Histochemistry
B Henderson

Abstract

A system has been developed for the quantitative measurment of glyceraldehyde 3-phosphate dehydrogenase activity in tissue sections. An obstacle to the histochemical study of this enzyme has been the fact that the substrate, gylceraldehyde 3-phosphate, is very unstable. In the present system a stable compound, fructose 1, 6-diphosphate, is used as the primary substrate and the demonsatration of the glyceraldehyde 3-phosphate dehydrogenase activity depends on the conversion of this compound into the specific substrate by the aldolase present in the tissue. The characteristics of the dehydrogenase activity resulting from the addition of fructose 1, 6-diphosphate, resemble closely the known properties of purified glyceraldehyde 3-phosphate dehydrogenase. Use of polyvinyl alcohol in the reaction medium prevents release of enzymes from the sections, as occurs in aqueous media. Although in this study intrinsic aldolase activity was found to be adequate for the rapid conversion of fructose 1, 6-diphosphate into the specific substrate for the dehydrogenase, the use of exogenous aldolase may be of particular advantage in assessing the intergrity of the Embden-Meyerhof pathway.

Mentioned in this Paper

Fructose
Enzymes, antithrombotic
Accessory Atrioventricular Bundle
Phosphate Measurement
NADH
Fructosephosphates
Enzymes for Treatment of Wounds and Ulcers
Formazans
Fructosediphosphate Aldolase
Glyceraldehyde-3-Phosphate Dehydrogenases

About this Paper

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