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. 1999 Sep 6;146(5):917–928. doi: 10.1083/jcb.146.5.917

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© 1999 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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p193 exists in cells associated with vaults and in other subcellular fractions. Comparison of levels of p193 during biochemical fractionation of HeLa cells. (A) Cellular protein fractions, nuclear (N), supernatant S100 (S), and microsomal pellet P100 (P) were generated from HeLa extracts and resolved by SDS-PAGE (see Materials and Methods). Immunoblot analysis was carried out using affinity-purified polyclonal antibody prepared against recombinant p193 fragment. (B) The P100 fraction was further fractionated on a discontinuous sucrose gradient (20/30/40/45/50/60%), and the proteins from the gradient fractions were resolved by SDS-PAGE. Immunoblot analysis was carried out using either affinity-purified p193 polyclonal antibody (top) or affinity-purified anti-vault polyclonal antibody (bottom). Sucrose gradient fraction sources are indicated at the top. P100 represents the starting material, and the vault sample was purified from rat liver (a lighter exposure of the detected MVP in purified vaults is shown). Arrows indicate the positions of p193 and MVP.