摘要
HFG (human fibrinogen) desorbed from a PTFE (polytetrafluoroethylene) surface and thermally denatured HFG were conformationally studied by using FTIR (Fourier transform infrared) spectroscopy. It is shown that some irreversible conformational changes of HFG, including a decrease in the α helix content and an increase in the β structure content, were induced by the PTFE surface adsorption/desorption.This suggests that some α helix structures should transform into β structures.Desorbed HFG was thermally denatured as well as the native HFG under a thermal incubation of 30 min at 73 ℃ .After the same thermal treatment, the α helix content in the thermally denatured desorbed HFG was obviously less than that in the former native HFG.
HFG (human fibrinogen) desorbed from a PTFE (polytetrafluoroethylene) surface and thermally denatured HFG were conformationally studied by using FTIR (Fourier transform infrared) spectroscopy. It is shown that some irreversible conformational changes of HFG, including a decrease in the α helix content and an increase in the β structure content, were induced by the PTFE surface adsorption/desorption.This suggests that some α helix structures should transform into β structures.Desorbed HFG was thermally denatured as well as the native HFG under a thermal incubation of 30 min at 73 ℃ .After the same thermal treatment, the α helix content in the thermally denatured desorbed HFG was obviously less than that in the former native HFG.
