Abstract
Factor XIIIa (FXIIIa), the blood coagulation enzyme, functions as a transglutaminase to covalently stabilize fibrin clots by introducing γ-glutamyl-e-lysyl peptide bonds between fibrin molecules (for detailed reviews, see references 1 and 2). The FXIII proenzyme exists in two zymogenic forms.3 Extracellular or plasma FXIII is composed of two subunits, A(Mr =80,500)4 and B(M =76,500),5 associated non-covalently as a tetrameric complex, A2B2.6,7 Intracellular FXIII is a dimer of only A subunits, A2.6 The A chains in both zymogens are identical and contain the active center sulfhydryl group.7,8 Upon activation by thrombin in the presence of calciurn ions, both zymogens give rise to the same enzymatic activity, FXIIIa.8,9
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