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. Author manuscript; available in PMC: 2020 Nov 1.
Published in final edited form as: J Mol Cell Cardiol. 2019 Sep 7;136:42–52. doi: 10.1016/j.yjmcc.2019.09.002

Figure 6: Similar affinities of mAb TnI-1 for HcTnI-C27 residing in SUMO fusion protein and in cardiac TnI.

Figure 6:

The ELISA titration curves normalized to maximum binding (A) showed that mAb TnI-1 binds its epitope in Tx3-SUMO-HcTnI-C27 fusion protein and in wild type cardiac TnI (cTnI) with similar affinities as reflected by the mAb TnI-1 dilutions for 50% maximum binding (B), which were similarly decreased by the R to H single amino acid substitution in Tx3-SUMO-HcTnI-C27-H fusion protein and in situ in R192H RCM mutant cardiac TnI (*P < 0.005 compared with the wild type control in Student’s t test).