Crystalline lactic dehydrogenase from heart muscle
- 1 April 1940
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 34 (4) , 483-486
- https://doi.org/10.1042/bj0340483
Abstract
The enzyme, which catalyses the reversible reduction of cozymase by lactic acid in animal tissues, was prepared in crystalline form. Starting from the water extract of bullock''s heart tissue, the procedure is adsorption to Ca3(PO4)2; elution with phosphate buffer; precipitation with (NH4)2SO4; precipitation with acetone; fractionation with (NH4)2SO4 between 0.3-0.5 saturation; precipitation with acetone; and crystallization from (NH4)2SO4. Colorless needles result which dissolve readily in water. The pure enzyme is inactivated if dialyzed against distilled water. On the addition of pure heart flavoprotein [see B. A. 13 (9): entry 14780] and cozymase, this crystalline enzyme catalyses the reduction of methylene blue by lactic acid. Lactic and malic dehydrogenases are not identical.This publication has 6 references indexed in Scilit:
- Isolation and properties of a flavoprotein from heart muscle tissueBiochemical Journal, 1939
- On the catalytic function of heart flavoproteinBiochemical Journal, 1939
- Coenzyme factor—a new oxidation catalystBiochemical Journal, 1938
- Identity of lactic and malic dehydrogenasesBiochemical Journal, 1937
- The malic dehydrogenase of animal tissuesBiochemical Journal, 1936
- The lactic dehydrogenase of animal tissuesBiochemical Journal, 1936