Cross-Linking of Bovine Fibrinogen with Formaldehyde.

Decomposition of trimethylamine oxide and changes in protein extractability during frozen storage of minced and intact hake (Merluccius productus) muscle

“…The FA formed during the reduction of TMAO to DMA may be rapidly interacting with the myofibrillar protein in a manner similar to the cross-linking with bovine fibrinogen described by Mihalyi (1963). The interaction of FA with myofibrillar protein could explain, in part, the undesirable textural changes that occur during the frozen storage of Pacific hake.…”

Development of fibrinogen microspheres as a biodegradable carrier for tissue engineering

“…Number of bifunctional cross-linking reagents, making covalent bond between amino and carboxyl group, were applied in various applications in protein chemistry 23 . The soluble Fbg could be cross-linked by natural thrombin and plasma transglutaminase activations, or by chemicals, like EDC, NHS, and aldehydes, such as formaldehyde 24 , glutaraldehyde 25 and genipin 26 . Since some chemicals could leach toxic byproducts upon degradation, EDC was selected as a cross-linking agent with hypothesis to maintain the basic functions of Fbg with other biological molecules 27 .…”

Fibrinogen and fibrin based micro and nano scaffolds incorporated with drugs, proteins, cells and genes for therapeutic biomedical applications

“…99 A few years later, in 1975, human Fbg cross-linking was introduced by Furlan and Beck, using glutaraldehyde and tetranitromethane. They further confirmed the participation of different chains (α, β, and γ) in intermolecular cross-linking, by performing sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the results of which evidenced that enhanced intermolecular cross-linking occurred when high concentrations of glutaraldehyde were used.…”

“…106 Tissue plasminogen activator can activate plasminogen to active plasmin (serine protease), which in turn, degrades Fbg and Fbn by cleaving the carboxyl terminal peptide bond of the Arginine or Lysine residues; therefore, for long-term degradation there needs to be an increase in the number of peptide bonds with suitable cross-linking agents. 99,101,102 Various studies have disclosed the potential of Fbg and Fbn scaffolds for cell viability, gene expression, and ECM production. However, to obtain better tissue engineering results, scaffolds should maintain their size and shape for prolonged periods, and to achieve that, it is necessary that they be stabilized with an appropriate cross-linking agent.…”