Two-state irreversible thermal denaturation of Euphorbia characias latex amine oxidase.
Thermal denaturation of Euphorbia latex amine oxidase (ELAO) has been studied by enzymatic activity, circular dichroism and differential scanning calorimetry. Thermal denaturation of ELAO is shown to be an irreversible process. Checking the validity of two-state it really describes satisfactorily the thermal denaturation of ELAO. Based on this model we obtain the activation energy, parameter T(*) (the absolute temperature at which the rate constant of denaturation is equal to 1 min(-1)), and total enthalpy of ELAO denaturation. HPLC experiments show that the thermal denatured enzyme conserves its dimeric state. The N(2)-->kD(2) model for thermal denaturation of ELAO is proposed: where N(2) and D(2) are the native and denatured dimer, respectively.
Amani
Mojtaba
M
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
Moosavi-Movahedi
Ali A
AA
Floris
Giovanni
G
Mura
Anna
A
Kurganov
Boris I
BI
Ahmad
Faizan
F
Saboury
Ali A
AA
D006631:Amine Oxidase (Copper-Containing) / Q000737:chemistry*; D028481:Euphorbia / Q000201:enzymology*; D007700:Kinetics; D007840:Latex; D010940:Plant Proteins / Q000737:chemistry; D011489:Protein Denaturation; D013696:Temperature; D013816:Thermodynamics
D007840:Latex; D010940:Plant Proteins; D006631:Amine Oxidase (Copper-Containing)