[Study on secondary structure and properties of alpha- and gamma-forms of human thrombin].

@article{Shvachko2006StudyOS,
  title={[Study on secondary structure and properties of alpha- and gamma-forms of human thrombin].},
  author={L P Shvachko and S V Litvinovich and V. K. Kibirev},
  journal={Ukrains'kyi biokhimichnyi zhurnal},
  year={2006},
  volume={78 1},
  pages={87-93}
}
Secondary structure and enzymatic properties of human a-thrombin and its gamma-form (obtaining during autolysis of the native enzyme) have been studied by differential scanning calorimetry (DSC) and circular dichroism (CD). According to DSC-data both alpha-thrombin and gamma-thrombin contained only one thermal transition peak at 58.5 and 53.3 degrees C, respectively. A comparison of these values suggested that gamma-form is less stable than initial a-thrombin. In contrast to that the thermogram… CONTINUE READING