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. 2000 Oct 16;151(2):425–438. doi: 10.1083/jcb.151.2.425

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Processing of HA truncation mutants. (A) Chymotrypsin (C) or trypsin (T) treated CV-1 cells were biotinylated, lysed, immunoprecipitated with the Site A antibody, resolved by SDS-PAGE, transferred to nitrocellulose, and visualized with streptavidin-HRP. Like WT HA, all mutant HAs exhibit efficient processing. (B) CV-1 cells were metabolically labeled, treated with trypsin, lysed, immunoprecipitated with an HA-specific mAb, treated with 1 U of N-Glycosidase F for 2 h at 37°C, and resolved on 15% SDS-PAGE. The gels were dried and exposed to film. Δ2–12 HA exhibit a mobility shift indicative of a truncated HA2 subunit (HA2*).