Compact residual structure in lentil lectin at pH 2.
Lentil lectin obtained from Lens culinaris collected in the La Armuña area (Salamanca, Spain) was examined by high-sensitivity differential scanning calorimetry, fluorimetry and measurements of circular dichroism at pH 2.0 and 7.4. At pH 2.0 the lentil lectin is not in the native state; however, at this pH it does show signs of a residual structure that breaks down upon heating. The lentil lectin at pH 2 shares some similarities with what has become known as the molten globule state. The thermal denaturation of intact (pH 7.4) and partially unfolded (pH 2.0) lentil lectin was irreversible and strongly dependent upon the scan rate, suggesting that its denaturation is under kinetic control. The process of lentil lectin denaturation is interpreted in terms of the simple kinetic model, Nk --> 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.
Marcos
M J
MJ
Departamento de Bioquímica y Biología Molecular, Universidad de Salamanca, Spain.
Villar
E
E
Gavilanes
F
F
Zhadan
G G
GG
Shnyrov
V L
VL
D002152:Calorimetry, Differential Scanning; D002236:Carbohydrate Conformation; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D037102:Lectins / Q000737:chemistry*; D037121:Plant Lectins; D013050:Spectrometry, Fluorescence; D013696:Temperature
D037102:Lectins; D037121:Plant Lectins; C033619:lentil lectin