pH‐dependent thermal transitions of lentil lectin

FEBS Letters

Marcos, Marı́a J.²  Zhadan, Galina G.²  L. Arrondo, Jose¹  L. Shnyrov, Valery²  Villar, Enrique²  Chehı́n, Rosana¹ 

[1]Departamento de Bioquı́mica, Universidad del Paı́s Vasco, P.O. Box 644, 48080 Bilbao, Spain

[2]Departamento de Bioquı́mica y Biologı́a Molecular, Universidad de Salamanca, Plaza de los Doctores de la Reina, s/n, 37007 Salamanca, Spain

关键词: Lentil lectin;    Irreversible thermal denaturation;    Differential scanning calorimetry;    Infrared spectroscopy;    Arrhenius equation;   

DOI  :  10.1016/S0014-5793(98)01708-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown