The inhibition of blood clotting by degradation products of fibrinogen reflects an interference
with fibrin network formation. The original discovery that digestion of fibrinogen by plasmin …

The fibrin polymers formed in solution during the earliest phase of the fibrinogen–fibrin
conversion are shown to be stable soluble molecules at pH7. 4 and 0.15 m-or 0.3 m-NaCl …

D. Knoll, 1 R. Hantgan,® J. Williams, 11J. McDonagh, 1 and J. Hermans* abstract:
Polymerization of fibrin is inhibited in the presence of excess fibrinogen fragment D. This …

The present day concept of the primary structure of fibrinogen is outlined. Cleavage of the
molecule with CNBr and plasmin has yielded a number of fragments which account for …

Department of Biochemistry, Temple University School of Medicine, Philadelphia,
Pennsylvania 19140 Received June 18, 1991; Revised Manuscript Received February 24 …

The mechanism of association and the organization of human fibrin were studied by using
affinity chromatography. Insolubilized fibrinogen, fibrin monomer, and crosslinked fibrin were …

Fibrinogen is a complex multifunctional protein comprised of three major domains (two outer
D and one central E) which contains constitutive binding sites (eg Da, Db,[gamma] XL, D …

During cleavage of fibrinogen by thrombin, fibrinopeptide A (FpA) release precedes
fibrinopeptide B (FpB) release. To examine the basis for this ordered release, we …

Gerald F. Smith** and Nils U. Bang abstract: Two new findings are presented in this
report:(1) it was discovered that a low thrombin activity can convert fibrinogen (1-2 and 1-8) …

Generation of a fibrin clot from purified thrombin and fibrinogen is initiated by a proteolytic
reaction and proceeds by means of three reversible 1-6 steps: the thrombin-induced …