Research article
Protein engineering of conger eel galectins by tracing of molecular evolution using probable ancestral mutants
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* Corresponding author: Tomohisa Ogawa ogawa@biochem.tohoku.ac.jp
1 Department of Biomolecular Science, Graduate School of Life Sciences, Tohoku University, Sendai 981-8555, Japan
2 Nagahama Institute of Bio-Science and Technology and Japan Science and Technology Agency, BioInfomatic Research Division, Nagahama, Shiga 526-0829, Japan
BMC Evolutionary Biology 2010, 10:43 doi:10.1186/1471-2148-10-43
Published: 14 February 2010Additional files
Additional file 1:
Table S1 - Con-anc mutants in this report. * For example, E5Q indicates that Glu5 of Con-anc substituted to corresponding ConI residue, Gln.
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Additional file 2:
Table S2 - Primer list in this report. * Upper is sense primer and lower is antisense primer in each row. The substitution sites were underlined, and unique restriction enzyme sites were in italics.
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Additional file 3:
Figure S1 - Schematic representation of PA oligosaccharides used in FAC analysis. 01-23, N-linked glycans; 26-50, glycolipid glycans. The reducing terminal sugar of each carbohydrate was pyridylaminated. All PA oligosaccharides were purchased from TaKaRa Bio (Kyoto, Japan). The numbers assigned to them are based on their product numbers. Each vertex of a hexagon indicates the position of the anomeric carbons in each monosaccharide. Thin pink and thick black lines represent α and β bonds, respectively. Glc, glucose; Gal, galactose; Man, mannose; Fuc, fucose; GlcNAc, N-acetylglucosamine; GalNAc, N-acetylgalactosamine; NeuAc, N-acetylneuraminic acid; and NeuGc, N-glycolylneuraminic acid.
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