Document Detail


Rheology of fibrin clots. III. Shear creep and creep recovery of fine ligated and coarse unligated closts.
MedLine Citation:
PMID:  974229     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Creep and creep recovery of human fibrin clots in small shearing deformations have been investigated over a time scale from 24 to 10(4) s. Coarse, unligated clots and fine clots ligated by fibrinoligase in the presence of calcium ions were studied to suppliement previous data on coarse ligated and fine unligated clots. Stress was found to be proportional to strain up to at least a maximum shear strain (in torsion geometry) of 6.2%. The initial modulus (25 s after imposition of stress) is proportional to approximately the 1.5 power of concentration for fine ligated and coarse unligated clots. For fine unligated closts there is comparatively little creep subsequent to the initial deformation; ligation (in this case involving mostly the gamma chains) reduces the creep to nearly zero. For coarse unligated clots, there is substantially more creep under constant stress, and creep recovery is not complete. Ligation (in this case involving both camma and alpha chains) alrgely supresses the creep and causes the recovery to be complete. If the structure if fully formed before creep begins, tests of creep recovery by the Boltzmann superposition principle show adherence to linear visoelastic behavior for all four clot types. Otherwise, the Boltzmann test fails and the recovery is much less than calculated. For fine ligated clots, the observed recovery agrees well with that calculated on the basis of a dual structure model in which an additional independent structure is built up in the deformed state, so that the state of ease after removal of stress is a balance between two structures deformed in opposite senses. It is postulated that the coherence and elastic modulus of the fine ligated clot are largely due to steric blocking of long protofibrils with a high flexural stiffness. In the coarse clot, it is proposed that the structure involves extensive branching of thick bundles of protofibrils, which become permanently secured by the ligation of the alpha chains of the fibrin.
Authors:
G W Nelb; C Gerth; J D Ferry
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biophysical chemistry     Volume:  5     ISSN:  0301-4622     ISO Abbreviation:  Biophys. Chem.     Publication Date:  1976 Sep 
Date Detail:
Created Date:  1977-01-03     Completed Date:  1977-01-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0403171     Medline TA:  Biophys Chem     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  377-87     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Blood Coagulation
Fibrin*
Humans
Macromolecular Substances
Mathematics
Protein Binding
Stress, Mechanical
Chemical
Reg. No./Substance:
0/Macromolecular Substances; 9001-31-4/Fibrin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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