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. 2007 Apr 9;177(1):29–37. doi: 10.1083/jcb.200611079

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Copyright © 2007, The Rockefeller University Press

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Figure 2. — Donor substrate selection from an OS-PP-Dol library. The purified yeast OST (A) or detergent extracts prepared from T. cruzi (B), T. vaginalis (C), C. neoformans (D), or E. histolytica (not depicted) membranes were assayed for OST activity in the presence of glucosidase and mannosidase inhibitors using 1.2 μM OS-PP-Dol and 10 μM tripeptide acceptor (Nα-Ac-N-[¹²⁵I]-Y-T NH₂). Glycopeptide products ranging in size between M₃GN₂-NYT (M3) and G₃M₉GN₂-NYT (G3) were resolved by HPLC and identified by migration relative to authentic standards (M5, M9, and G3). (E and F) The normalized initial transfer rate (OS-NYT/OS-PP-Dol) for the eight most abundant OS-PP-Dol donors was calculated by dividing the composition of the glycopeptide products by the composition of the OS-PP-Dol donor library. The OST from all organisms was assayed twice to determine the composition of the product pool. The composition of the donor pool was determined by duplicate assays (Fig. S1, available at http://www.jcb.org/cgi/content/full/jcb.200611079/DC1). Note the difference in ordinate scales for E and F.