D-Glyceraldehyde-3-Phosphate Dehydrogenase. The Purification and Characterisation of the Enzyme from the Thermophiles Bacillus stearothermophilus and Thermus aquaticus
- 1 July 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 108 (2), 535-547
- https://doi.org/10.1111/j.1432-1033.1980.tb04750.x
Abstract
D-Glyceraldehyde-3-phosphate dehydrogenase from 2 thermophilic bacteria was purified by procedures including affinity chromatography on NAD+-Sepharose. Methods for making NAD+-free enzyme are also described. Both the holo and apo forms of the enzyme from B. stearothermophilus were crystallized. The enzymes are tetrameric and composed of 4 chemically identical polypeptide chains of MW 36,000. The enzymes are much more stable to heat than their counterparts from mesophiles.This publication has 47 references indexed in Scilit:
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