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. 2000 Jul 10;150(1):119–130. doi: 10.1083/jcb.150.1.119

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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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Nondenaturing PAGE of 26S proteasomes. Fractions 10, 13, 16, and 19 (40 μl) from the sucrose gradients were electrophoresed for 800 V-h on 4.5% native polyacrylamide gels. a, Proteolytic activity of the resolved complexes was detected by fluorogenic peptide overlay with Suc-LLVY-AMC and the proteins were visualized by Coomassie blue stain (b; same gel). c, To further characterize the bands, duplicate samples of fraction 19 were transferred to nitrocellulose membranes and immunostained with μ3/50, an mAb directed against the RC subunit, p39A, and with another, V.D5, directed against the 20S proteasome. The analysis of a, b, and c allowed unambiguous identification of the bands as 20S proteasomes, RCs, 26S proteasomes with only one RC attached (20S-RC₁), and 26S proteasomes with two RCs (20S-RC₂), as indicated.