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Updated: Aug 10, 2026

Experimental and Imaging Techniques for Examining Fibrin Clot Structures in Normal and Diseased States
Published on: April 1, 2015
Thermally induced conformational changes in fibrin film
1Department of Chemistry, University of Wisconsin, Madison 53706.
Abstract:
Fibrin film is prepared by compaction in one dimension of a fibrin clot (pH 6.3, ionic strength 0.15, fibrin concentration about 0.5%) by expulsion of fluid to reach a fibrin concentration of about 15%. Strips of film, equilibrated in the same buffer with very slowly increasing temperature, shrink in length in a narrow temperature range, as reported in 1962 by Loeb and Scheraga. The transition temperature was found to be 54 +/- 2 degrees C independently of whether the film was unligated or ligated (cross-linked) by Factor XIIIa and whether the film had previously undergone stretching with about 50% stress relaxation at a relative length of 1.23 to 1.44 and subsequent stress-free retraction. The percentage of linear shrinkage in buffer was about 32%. The transition corresponds to that observed calorimetrically by Mihalyi and Donovan in both fibrinogen and fibrin and by Medved' and Privalov in fibrinogen, localized in the D fragment. It is attributed to unfolding of structures in the D domain.
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