Differential scanning calorimetric study of the thermal denaturation of aspartate transcarbamoylase of Escherichia coli

Biochemistry ◽  
1988 ◽  
Vol 27 (21) ◽  
pp. 8081-8087 ◽  
Author(s):  
Victoria Edge ◽  
Norma M. Allewell ◽  
Julian M. Sturtevant
1994 ◽  
Vol 299 (3) ◽  
pp. 731-733 ◽  
Author(s):  
G G Zhadan ◽  
V L Shnyrov

A differential-scanning-calorimetric study of the thermal denaturation of a sea-anemone (Radianthus macrodactylus) 8 kDa cytolytic toxin was carried out. The calorimetric traces were found to be irreversible and scan-rate-dependent under the experimental conditions employed. Scan-rate-dependent thermograms were explained in terms of a two-state kinetic model N k -->D, where k is a first-order kinetic constant that changes with temperature as given by the Arrhenius equation, N is the native state of the toxin, and D the denatured one.


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