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. 2010 May 31;189(5):829–841. doi: 10.1083/jcb.200912105

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© 2010 Pearse et al.

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 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 6. — Hydropathic profiles of mouse prosaposin glycan regions. The hydropathic profiles of the amino acids C-terminal to the N-glycans of prosaposin are depicted. Kyte-Doolittle values were used in calculating the mean hydrophobicity with a window size of 3 aa. The Asn residue for each N-glycan is positioned at 0 on the plots. Note that the C and D glycans of prosaposin possess the oscillating hydrophobicity profiles associated with efficient reglucosylation by UGT1 (Taylor et al., 2003). Positive values indicate hydrophobicity.