@article{oai:u-ryukyu.repo.nii.ac.jp:02015643,
 author = {Inoue, Fumihide and Nakada, Fukuichi},
 issue = {1},
 journal = {琉球大学医学会雑誌 : 医学部紀要 = Ryukyu medical journal},
 month = {},
 note = {Sedimentation coefficient, S^0_<20,w> of human fibrinogen-stearyltrimethylammonium chloride, FG-STA(C1), was dependent on pH and the values were found to be 14.3 and 7.2 s at pH 5.8 and 3.8, respectively. Circular dichroism spectra of FG-STA(C1) showed the presence of $ \alpha $-helix (from a double minimum) at between pH 5.8 and 3.8. The molar ellipticity at 222nm were calibrated to be  $-10,025 \pm 450$ and $-13,000 \pm 600$ degree・ cm^3・decimole^<-1> at pH 5.8 and 3.8, respectively. It can be suggested that STA-C1 bound to fibrinogen alter the surface character of the protein. Action of STA-C1 is not to denature fibrinogen, but to maintain the conformational structure of the protein., 論文},
 pages = {6--11},
 title = {[原著］Physicochemical Properties of Human Fibrinogen-Cationic Detergent Complex},
 volume = {6},
 year = {1983}
}