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Full-Text Articles in Medicine and Health Sciences
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 …
Evidence For Intramolecular Cross-Linked Aα·Γ Chain Heterodimers In Plasma Fibrinogen, Kevin R. Siebenlist, Michael W. Mosesson
Evidence For Intramolecular Cross-Linked Aα·Γ Chain Heterodimers In Plasma Fibrinogen, Kevin R. Siebenlist, Michael W. Mosesson
Biomedical Sciences Faculty Research and Publications
A peptide band of ∼105 kDa migrating near the γ dimer position of disulfide bond reduced human plasma fibrinogen prepared from fresh single donor or outdated plasma was identified by SDS−PAGE. The band, amounting to ∼2% of the total Aα/γ chain population, was thrombin and plasmin sensitive and reacted with antibodies to Aα or γ chains but not with antibodies to Bβ chains, plasminogen, or factor XIII. Amino acid sequencing revealed a double sequence corresponding to that of Aα and γ chains, indicating that the band consists of covalently cross-linked Aα·γ chain heterodimers. Aα·γ heterodimers were identified as a component …