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. 2007 Feb 26;402(Pt 3):503–513. doi: 10.1042/BJ20061064

Table 1. Catalytic parameters for the enzymatic processing at 37 °C and pH 7.1 of native fibrinogen by the whole MMP-2, the catalytic domain of MMP-2 and plasmin and of peroxynitrite-treated fibrinogen by whole MMP-2.

kcat/Km (M−1·s−1) kcat (s−1) Km (M)
α-Chain
 Native fibrinogen
  Whole MMP-2 2.29(±0.23)×105 36.4(±4.2) 1.59(±0.18)×10−4
  Catalytic domain 1.09(±0.12)×104 0.19(±0.02) 1.72(±0.19)×10−5
   MMP-2
  Plasmin 2.04(±0.21)×105 7.7(±0.9) 3.77(±0.41)×10−5
 Oxidized fibrinogen
  Whole MMP-2 1.05(±0.11)×105 3.1(±0.4) 2.93(±0.35)×10−5
β-Chain
 Native fibrinogen
  Whole MMP-2 6.61(±0.83)×104 12.5(±1.4) 1.89(±0.20)×10−4
  Catalytic domain 3.59(±0.42)×103 0.12(±0.02) 3.27(±0.41)×10−5
   MMP-2
  Plasmin 2.47(±0.34)×105 27.8(±2.9) 1.12(±0.15)×10−4
 Oxidized fibrinogen
  Whole MMP-2 1.34(±0.15)×105 1.06(±0.12) 7.93(±0.88)×10−6
γ-Chain
 Native fibrinogen
  Plasmin 4.96(±0.6)×104 2.35(±0.36) 4.74(±0.57)×10−5