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pH‐dependent thermal transitions of lentil lectin
Author(s) -
Marcos Marı́a J.,
Chehı́n Rosana,
L. Arrondo Jose,
Zhadan Galina G.,
Villar Enrique,
L. Shnyrov Valery
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01708-6
Subject(s) - arrhenius equation , chemistry , differential scanning calorimetry , kinetic energy , denaturation (fissile materials) , kinetics , thermodynamics , lectin , reaction rate constant , thermal stability , activation energy , analytical chemistry (journal) , chromatography , biochemistry , nuclear chemistry , organic chemistry , physics , quantum mechanics
The thermal stability of lentil lectin in the 5.0–10.0 pH range was studied by high‐sensitivity differential scanning calorimetry and infrared spectroscopy. The thermally induced transitions for protein were irreversible and strongly dependent upon the scan rate at all pH values, suggesting that the denaturation is under kinetic control. It is shown that process of lentil lectin denaturation can be interpreted with sufficient accuracy in terms of the simple kinetic scheme, , where k is a first‐order kinetic constant that changes with temperature, as given by the Arrhenius equation, N is the native state, and D is the denatured state. On the basis of this model, the parameters of the Arrhenius equation were calculated.