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Quasielastic light‐scattering studies on human fibrinogen and fibrin. I. Fibrinogen
Author(s) -
Palmer G. R.,
Fritz O. G.,
Hallett F. R.
Publication year - 1979
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1979.360180705
Subject(s) - chemistry , fibrinogen , diffusion , fibrin , molecule , denaturation (fissile materials) , light scattering , ionic strength , scattering , thermodynamics , organic chemistry , nuclear chemistry , optics , biochemistry , physics , biology , aqueous solution , immunology
Abstract A quasielastic light‐scattering system has been constructed to study human fibrinogen. The first phase of the investigation was an attempt to clarify the shape of the firbinogen molecule using diffusion methods. The translational diffusion coefficient was measured as 2.04 ± 0.09 × 10 −7 cm 2 sec −1 . Aggregation is suggested as the reason for a lower value previously obtained using this technique. Diffusion indicated the molecule was rigid and did not dissociate at low concentration, low ionic strength, or 37°C. Thermal denaturation was observed at 40°C. At 3°C, a second thermal instability was discovered.