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. 1978 Jun;75(6):2584-7.
doi: 10.1073/pnas.75.6.2584.

Proposed temperature-dependent conformational transition in D-amino acid oxidase: a differential scanning microcalorimetric study

J M Sturtevant, P L Mateo

Proposed temperature-dependent conformational transition in D-amino acid oxidase: a differential scanning microcalorimetric study

J M Sturtevant et al. Proc Natl Acad Sci U S A. 1978 Jun.

Abstract

A number of authors have reported observations on D-amino acid oxidase [D-amino acid: O2 oxidoreductase (deaminating), EC 1.4.3.3.] that they have interpreted in terms of a temperature-dependent conformational transition having a van't Hoff enthalpy amounting to more than 1 cal per g of protein (1 cal = 4.184J). No indication of this transition is obtained by using a differential scanning calorimeter having a sensitivity considerably in excess of that required to detect such a transition. The implications of this discrepancy are discussed.

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References

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