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- W2946180372 abstract "Copperhead venom procoagulant enzyme, previously shown to remove fibrinopeptide B at faster rate than fibrinopeptide A, has been found to release little of the A peptide at temperatures below 14°. At low temperatures, tight aggregation of the derivative lacking B blocked release of A by the enzyme. Transient release of A occurred, but stopped as removal of B approached completion. Overall losses of A amounted to 8% and 2% from human and rabbit fibrinogen respectively. Resultant clots with A intact dissolved on warming to 37°, whereafter release of A resumed with secondary coagulation ensuing. When dissolved at 37° with PMSF-inactivated enzyme, the fibrin remained highly soluble (>12 mg/ml). Ultracentrifugation showed constant levels of 8S monomer together with 16S aggregates in amounts accounting for the total protein at concentrations down to 0.16 mg/ml, and monomer alone at lower concentrations. From changes in saturation level of monomer at lower temperatures, the enthalpy of aggregation appeared to be about half of the -50 kcal/mole associated with aggregation of regular fibrin. Other experiments indicate that removal of the A and B peptides unmasks separate aggregation sites, each of which place the monomers in alignment suitable for rapid crosslinking. The β-chain segment spanning residues 15-42 appears to be critically involved in the aggregation that follows release of B itself, because the aggregation does not occur when this segment is removed together with B in early stages of reaction between fibrinogen and plasmin. The aggregation which follows release of A depends on a different site, because the early alterations inflicted by plasmin do not prevent coagulation of fibrinogen by thrombin. (Supported in part by USPHS Grant HL-16361)." @default.
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- W2946180372 date "1977-01-01" @default.
- W2946180372 modified "2023-09-23" @default.
- W2946180372 title "Fibrinopeptide B and Aggregation of Fibrinogen" @default.
- W2946180372 doi "https://doi.org/10.1055/s-0039-1680595" @default.
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