Vl. Shnyrov et al., KINETIC-STUDY ON THE IRREVERSIBLE THERMAL-DENATURATION OF LENTIL LECTIN, Biochemistry and molecular biology international, 39(4), 1996, pp. 647-656
The irreversible thermal denaturation of lentil lectin was investigate
d at pH 7.4 using different techniques including high-sensitivity diff
erential scanning calorimetry, differential detergent solubility therm
al gel analysis, intrinsic fluorescence and hemagglutinating activity
assays. The shape of the transition, as well as its scan-rate dependen
ce, can be explained by assuming that thermal denaturation takes place
according to the kinetic scheme N (k)--> D, where k is a first-order
kinetic constant that changes with temperature, as given by the Arrhen
ius equation, N the native state, and D the denatured one. On the basi
s of this model, the value of the rate constant as a function of tempe
rature and the activation energy were calculated. The analytical data
obtained with the other methods used in this work support the proposed
two-state kinetic model.