pH-dependent thermal transitions of lentil lectin.
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, N-->D, 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.
Marcos
M J
MJ
Departamento de Bioquímica y Biología Molecular, Universidad de Salamanca, Spain.
Chehín
R
R
Arrondo
J L
JL
Zhadan
G G
GG
Villar
E
E
Shnyrov
V L
VL
D002152:Calorimetry, Differential Scanning; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D037102:Lectins / Q000737:chemistry*; D037121:Plant Lectins; D013055:Spectrophotometry, Infrared; D013816:Thermodynamics