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. 2007 Aug 24;35(17):5809–5818. doi: 10.1093/nar/gkm613

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© 2007 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 7. — Pif1p exists as a monomer in solution. Pif1p was subjected to centrifugation through a 15–40% glycerol gradient. The protein markers used as molecular weight standards were Carbonic Anhydrase (29 kDa; s_20,w = 2.8 S), BSA (66 kDa, s_20,w = 4.41 S), ADH (150 kDa, s_20,w = 4.8 S), β-Amylase (200 kDa, s_20,w = 8.9 S) and Thyroglobulin (669kDa, s_20,w = 19.4 S). Two hundred and fifty micro liter fractions from the 5 ml gradient were analyzed for protein content by Coomassie gel staining to determine elution peak of molecular weight markers, and by anti-His western blotting for the detection of Pif1p.