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Article

Thermal unfolding of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase studied by differential scanning calorimetry.

Biochimica et biophysica acta - 17 Aug 1999

Levashov P, Orlov V, Boschi-Muller S, Talfournier F, Asryants R, Bulatnikov I, Muronetz V, Branlant G, Nagradova N

Abstract excerpt

Thermal unfolding parameters were determined for a two-domain tetrameric enzyme, phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and for its isolated NAD(+)-binding domain. At pH 8.0, the transition temperatures (t(max)) for the apoforms of the native Bacillus stearothermophilus GAPDH and the isolated domain were 78.3 degrees C and 61.9 degrees C, with calorimetric enthalpies (DeltaH(cal)) of...

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Identifiers

PMID: 10446379
DOI: 10.1016/s0167-4838(99)00132-6

Genes

GAPDH

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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