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. 2014 Dec 1;127(23):5014–5026. doi: 10.1242/jcs.151878

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© 2014. Published by The Company of Biologists Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.

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Fig. 2. — Computational model predicts galactosyltransferase controls glycan antennarity. In silico variation of local enzyme concentrations: (A) ManI; (B) ManII; (C) GnTI; (D) GnTII; (E) GnTIV; (F) GnTV; (G) GalT. Final concentrations of N-glycan structures of different antennarities predicted by the kinetic model are plotted as a function of the total concentration of GalT, when combined with a 25-fold overexpression of GnTIV and GnTV. The position of the arrow on each abscissa indicates the default enzyme concentration. Values on each ordinate axis are expressed as a molar percentage of the total concentration of all N-glycan forms.