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. Author manuscript; available in PMC: 2011 May 1.
Published in final edited form as: Biochem J. 2010 Apr 14;427(3):467–475. doi: 10.1042/BJ20091594

Table 1. Kinetic and equilibrium dissociation constants of the binding of transglutaminase-2 to endostatin.

Rate and affinity constants of the binding of soluble transglutaminase-2 to immobilized endostatin calculated from SPR binding assays using the Biacore T100 evaluation software 2.0.1.

Endostatin
(Immobilized on
the chip)
HEK 293 EBNA
cells
P. pastoris
Guinea pig TG-2
Injected in soluble
form
+ 2 mM CaCl2 + 2 mM CaCl2
ka (M−1s−1) 1.12×105 M−1 s−1 6.10 ×104 M−1 s−1
kd (s−1) 7.65×10−4 s−1 3.41×10−4 s−1
KD (M) 6.8 nM 5.59 nM
Chi2 4.1 8.81
U-value 1 1