Two-state irreversible thermal denaturation of muscle creatine kinase.
Thermal denaturation of creatine kinase from rabbit skeletal muscle has been studied by differential scanning calorimetry. The excess heat capacity vs. temperature profiles were independent of protein concentration, but strongly temperature scanning rate-dependent. It has been shown that thermal denaturation of creatine kinase satisfies the previously proposed validity criteria for the two-state irreversible model [Kurganov et al., Biophys. Chem.70 (1997) 125]. The energy activation value has been calculated to be 461.0 +/- 0.7 kJ/mol.
Lyubarev
A E
AE
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
Kurganov
B I
BI
Orlov
V N
VN
Zhou
H M
HM
D000818:Animals; D002152:Calorimetry, Differential Scanning; D003402:Creatine Kinase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D066298:In Vitro Techniques; D007700:Kinetics; D018482:Muscle, Skeletal / Q000201:enzymology*; D011489:Protein Denaturation; D011817:Rabbits; D013816:Thermodynamics
D003402:Creatine Kinase