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Full-Text Articles in Medicine and Health Sciences
Position Of Γ-Chain Carboxy-Terminal Regions In Fibrinogen/Fibrin Cross-Linking Mixtures, Kevin R. Siebenlist, David A. Meh, Michael W. Mosesson
Position Of Γ-Chain Carboxy-Terminal Regions In Fibrinogen/Fibrin Cross-Linking Mixtures, Kevin R. Siebenlist, David A. Meh, Michael W. Mosesson
Biomedical Sciences Faculty Research and Publications
There are conflicting ideas regarding the location of the carboxyl-terminal regions of cross-linked γ-chain dimers in double-stranded fibrin fibrils. Some investigators believe that the chains are always oriented longitudinally along each fibril strand and traverse the contacting ends of abutting fibrin D domains (“DD-long” cross-linking). Other investigations have indicated instead that the chains are situated transversely between adjacent D domains in opposing fibril strands (transverse cross-linking). To distinguish between these two possibilities, the γ dimer composition of factor XIIIa-cross-linked fibrin/fibrinogen complexes that had been formed through noncovalent D/E interactions between fibrinogen D domains and fibrin E domains was examined. Two …
Plasma Factor Xiii Binds Specifically To Fibrinogen Molecules Containing Γ‘ Chains, Kevin R. Siebenlist, David A. Meh, Michael W. Mosesson
Plasma Factor Xiii Binds Specifically To Fibrinogen Molecules Containing Γ‘ Chains, Kevin R. Siebenlist, David A. Meh, Michael W. Mosesson
Biomedical Sciences Faculty Research and Publications
The difference between peak 1 and peak 2 fibrinogen lies in their γ chains. Peak 1 molecules contain 2 γA chains; peak 2 molecules contain 1 γA and 1 γ‘ chain, the latter of which contains a 20 amino acid extension (γ‘ 408−427) replacing the carboxyl-terminal 4 amino acids of the γA chain (γA 408−411). While the existence of γ‘ chains in plasma fibrinogen molecules has been known for many years, their function remains unknown. When fibrinogen is purified from plasma, the factor XIII zymogen (A2B2) copurifies with it and is found only in the peak …