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Crosslinking of fibrinogen to immobilized DesAA-fibrin.
DesAA-fibrin Sepharose was produced by treating fibrinogen-Sepharose with batroxobin. DesAA-fibrin Sepharose was mixed with different concentrations of fibrinogen and at different ratios, and incubated with preactivated FXIII. After 2 hours at 37 degrees C, the Sepharose beads were separated by centrifugation and non-crosslinked fibrinogen was removed by twice times washing with guanidinium chloride, pH 4.1. Under these experimental conditions specific crosslinking of fibrinogen to immobilized desAA-fibrin by FXIIIa was found. These results support the concept of a specific interaction between fibrinogen and fibrin involving polymerization which enables FXIIIa to crosslink fibrin to fibrinogen being in an half-staggered overlap position but not in DD-long contact.
PMID: 4049326 [PubMed - indexed for MEDLINE]
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Cited by 3 PubMed Central articles
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Influence of a natural and a synthetic inhibitor of factor XIIIa on fibrin clot rheology
Ryan EA, Mockros LF, Stern AM, Lorand L.
Biophys J. 1999 Nov; 77(5):2827-36.
[Biophys J. 1999]
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The location of the carboxy-terminal region of gamma chains in fibrinogen and fibrin D domains.
Mosesson MW, Siebenlist KR, Meh DA, Wall JS, Hainfeld JF.
Proc Natl Acad Sci U S A. 1998 Sep 1; 95(18):10511-6.
[Proc Natl Acad Sci U S A. 1998]
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Identification of covalently linked trimeric and tetrameric D domains in crosslinked fibrin.
Mosesson MW, Siebenlist KR, Amrani DL, DiOrio JP.
Proc Natl Acad Sci U S A. 1989 Feb; 86(4):1113-7.
[Proc Natl Acad Sci U S A. 1989]