Study of thermal stability of cytochrome P450 by differential scanning calorimetry

FEBS Letters

Stružinský, Rudolf¹  Anzenbacher, Pavel²  Hudeček, Jiří³ 

[1] Instituteof Microbiology, Czechoslovak Academy of Sciences, Vídeňská 1083, 142 20 Prague 4, Czechoslovakia;Department of Biochemistry, Charles University, Albertov 2030, 128 40 Prague 2 Czechoslovakia;Physical Chemistry, Charles University, Albertov 2030, 128 40 Prague 2 Czechoslovakia

关键词: Cytochrome P450;    Protein denaturation;    Differential scanning calorimetry;    Thermal stability;    Protein structure;   

DOI  :  10.1016/0014-5793(82)81102-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Thermal denaturation of cytochrome P450 is shown to be a complex process which occurs in two steps. The first (about 50°C) takes place in several stages which can be attributed to denaturation of different regions in the cytochrome P450 with different stability. The second transition (about 90°C) is fully reversible and similar to those described for other hemoproteins.

【 授权许可】

Unknown