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. 2005 Aug 15;202(4):493–503. doi: 10.1084/jem.20042155

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Copyright © 2005, The Rockefeller University Press

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Figure 1. — Digitonin-solubilized TCR has an αβγɛδɛζζ stoichiometry. (A) Current structural models of the TCR complex. The minimal hexameric complex, which comprises one TCRα/β dimer (monovalent), and an alternative model with two TCRα/β dimers (bivalent) are shown. (B) The digitonin-solubilized TCR complex is of a defined size. TCRs from the sources indicated were prepared either by NIP elution from NP-Sepharose columns, from membrane fractions, or by phenylphosphate elution from antiphosphotyrosine affinity columns. After separation by BN-PAGE, immunoblotting was performed with an anti-ζ serum. As a control, the BCR was run in parallel and immunoblotted with an antilight chain serum. The marker protein in this and all subsequent BN-PAGEs is ferritin in its 24-mer, 48-mer, and 72-mer forms (f1, 440 kD; f2, 880 kD; and f3, 1,320 kD). (C) The digitonin-solubilized TCR contains two CD3 dimers. TCRs contained in total membrane fractions from human PBMCs (lanes 1–3) or in antiphosphotyrosine immunoprecipitates from CH7C17 T cells (lanes 4–6) were incubated with the amounts of the anti-CD3 (UCHT1) Fab fragments indicated and resolved by BN-PAGE. (D) The digitonin-solubilized complex contains one TCRβ subunit. TCRs prepared from antiphosphotyrosine immunoprecipitates of human PBMCs (lanes 1–3) or CH7C17 cells (lanes 4–5) were incubated with the anti-TCRβ antibodies Jovi1 (lanes 1–3) or Jovi3 (lanes 4–6) and resolved by BN-PAGE.