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. 2019 Aug 29;47:329–340. doi: 10.1016/j.ebiom.2019.08.045

Fig. 3.

Fig. 3

cTnImAbs as bioactive alternative for cTnIAAb.

a. Differential binding affinities of cTnImAb1, −2, and −3 for myocardial membrane as revealed by flow cytometry. cTnImAb1 exhibited the highest binding force.

b & c. Flow cytometry showed that cTnImAb1 was a potent competitor against human cTnIAAb in binding to the myocardial cell membrane. Shown are representative images (b) and quantification (c). *p = .000 (ANOVA analysis).

d. Differential binding affinities of cTnImAb1, −2 and −3 for the membranes of BCG823 cells as revealed by flow cytometry. cTnImAb1 exhibited the highest affinity.

e & f. Flow cytometry showed that cTnImAb1 was a potent competitor against human cTnIAAb in binding to the membrane of BCG823 cells. Shown are representative images (e) and quantification (f). *p = .000 (ANOVA analysis).