Primary Structure of Human Coagulation Factor XIII

  • Akitada Ichinose
  • Earl W. Davie
Part of the Advances in Experimental Medicine and Biology book series (NATO ASI F, volume 231)


Factor XIII (fibrin stabilizing factor or fibrinoligase) is a plasma transglutaminase that plays an important role in the final stages of blood coagulation and the regulation of fibrinolysis. The molecule occurs in blood as a tetramer, a 2 b 2 (about 320 kD), consisting of two a subunits (75 kD each) and two b subunits (80 kD each) as estimated by SDS-polyacrylamide gel electrophoresis (Schwartz et al., 1973; Chung et al., 1974) (Fig. 1). The molecular complex is held together by noncovalent bonds (Schwartz et al., 1973). During the final stage of blood coagulation, thrombin converts the proenzyme (factor XIII) to an active form (factor XIIIa) by releasing an activation peptide (4 kD) from the N-terminus of each of the a subunits (Schwartz et al., 1973; Takagi and Doolittle, 1974). This reaction is stimulated by fibrin monomers (Lewis et al., 1985). In the presence of calcium ions, the activated a dimer dissociates from the b dimer (Cooke and Holbrook, 1974; Chung et al., 1974; Lorand et al., 1974) and binds to fibrin more tightly. Fibrin also lowers the calcium concentration required for the release of the b dimer (Credo et al., 1981). Calcium binds to the a subunit and unmasks its active site (Curtis et al., 1974; Cooke, 1974).


Factor Xiii Blood Coagulation Factor Fibrin Monomer Human Blood Platelet Coagulation Factor Xiii 


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Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Akitada Ichinose
    • 1
  • Earl W. Davie
    • 1
  1. 1.Department of BiochemistryUniversity of WashingtonSeattleUSA

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