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. 2014 Apr 1;289(20):14360–14369. doi: 10.1074/jbc.M113.535609

TABLE 2.

Comparison of competition experiments between hCGβ, hLHβ, and LC Iβ chimeras

As diagrammed in Fig. 1, hLHβδ114 represents the human LHβ-subunit truncated at position 114. hLHβ-CGtail represents the human LHβ-subunit with amino acids from 114 to the C terminus replaced with those from hCG. LC Iβ-F2 is an analog containing 4 residues of hLHβ (residues 2, 8, 10, and 15) with the remaining components hCG except for residues 38–56 (where hCG residues have been replaced with those from hFSH). The α-subunit contains a cysteine in place of serine 43 in all assays. Analogs were co-transfected into COS-7 cells and quantified in A113/125I-B110 assays. “Total dimer” represents the total amount of dimer detected. “Cross-linked dimer” represents the amount of heterodimer that remained after pH 2 treatment, 30 min at 37 °C. “% cross-linked dimer” is the ratio of cross-linked dimer to total dimer. In all analogs that contain βC26A, the β-subunit has the cysteine at position 26 replaced by alanine.

Row no. Analogs Total dimer X-linked dimer % X-linked dimer
%
1 hLHβ 0.98 ± 0.04 0.21 ± 0.01 21
2 hCGβ 5.89 ± 0.61 0.67 ± 0.10 11
3 hLHβ C26A 0.47 ± 0.02 0.50 ± 0.02 100
4 hCGβ C26A 3.61 ± 0.17 3.41 ± 0.32 94
5 hLHβ + hLHβ C26A 0.40 ± 0.06 0.31 ± 0.04 78
6 hCGβ + hCGβ C26A 6.45 ± 0.62 1.26 ± 0.10 20
7 hLHβδ114 4.53 ± 0.18 0.43 ± 0.02 9
8 hLHβδ114 C26A 0.89 ± 0.07 0.94 ± 0.03 100
9 hLHβδ114 + hLHβδ114 C26A 0.81 ± 0.05 0.65 ± 0.05 80
10 hLHβ-CGtail 3.56 ± 0.20 0.46 ± 0.04 13
11 hLHβ-CGtail C26A 3.35 ± 0.48 3.53 ± 0.51 100
12 hLHβ-CGtail + hLHβ-CGtail C26A 3.16 ± 0.25 2.26 ± 0.30 72
13 LC Iβ-F2 0.89 ± 0.03 0.30 ± 0.01 34
14 LC Iβ-F2 C26A 1.12 ± 0.04 1.11 ± 0.02 99
15 LC Iβ-F2 + LC Iβ-F2 C26A 0.47 ± 0.02 0.37 ± 0.04 79