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. 1997 Dec 9;94(25):13838–13843. doi: 10.1073/pnas.94.25.13838

Table 2.

Affinities of the 2C TCR for its pMHC ligands

pMHC ligand 2C TCR Kass, (M−1⋅s−1 × 103) Kdiss, s−1 × 10−2 Kd, μM
Ld-p2Ca C-AB treated 8.30  ±  1.45 2.7  ±  0.4 3.3  ±  0.4
Ld-p2Ca Deglycosylated 9.40  ±  2.10 1.5  ±  0.2 1.6  ±  0.1
Ld-QL9 C-AB treated 6.35  ±  0.60 2.5  ±  0.4 3.9  ±  0.2
Ld-QL9 Deglycosylated 6.12  ±  0.65 1.2  ±  0.1 2.0  ±  0.2
Ld-MCMV C-AB treated NM NM NM
Ld-MCMV Deglycosylated NM NM NM
Kb-dEV8 C-AB treated 2.20  ±  0.45 18.5  ±  2.0 84.1  ±  12.0
Kb-SIYR C-AB treated 2.35  ±  0.85 7.5  ±  2.1 31.9  ±  6.2
Kb-VSV C-AB treated NM NM NM
Kbm3-dEV8 C-AB treated 0.85  ±  0.15 4.8  ±  0.4 56.5  ±  8.1
Kbm3-SIYR C-AB treated 2.65  ±  0.15 7.8  ±  0.9 29.4  ±  3.2
Kbm3-VSV C-AB treated NM NM NM

For the 2C TCR, C-AB indicates that the 2C has been carboxypeptidase A and B treated to trim the C-terminal tails, and deglycosylated indicates that the 2C TCR was expressed in the presence of tunicamycin and therefore was free of N-linked glycosylation (see Methods). Measurements were made by surface plasmon resonance on a BIAcore 2000 machine as detailed in Materials and Methods. NM, not measurable.