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Characterisation of oxidized recombinant human Galectin-1

Journal Article


Abstract


  • Oxidized human galectin-1 plays a role in the immune response to injured axons. Over-expression of galectin-1 by cancer, in combination with cancer associated oxidative stress suggests oxidized human galectin-1 may also play a role(s) in tumourigenesis. Here we generate milligram quantities of oxidized human galectin-1 and undertake biophysical characterization. The protein adopts a number of different states. Two separable oxidized forms are identified that exist as largely mono-disperse solutions at higher milligram/ml concentrations. The presence of disulphide bonds is confirmed for these two protein forms, as is their change in overall shape and loss of lectin activity. Our studies lead to production of a particular mono-disperse oxidized human galectin-1 species that is anticipated most optimal for investigations requiring milligram/ml concentrations such as X-ray crystallography. © 2009 Bentham Science Publishers Ltd.

Publication Date


  • 2009

Citation


  • Scott, S. A., Bugarcic, A., & Blanchard, H. (2009). Characterisation of oxidized recombinant human Galectin-1. Protein and Peptide Letters, 16(10), 1249-1255. doi:10.2174/092986609789071342

Scopus Eid


  • 2-s2.0-69549097373

Start Page


  • 1249

End Page


  • 1255

Volume


  • 16

Issue


  • 10

Abstract


  • Oxidized human galectin-1 plays a role in the immune response to injured axons. Over-expression of galectin-1 by cancer, in combination with cancer associated oxidative stress suggests oxidized human galectin-1 may also play a role(s) in tumourigenesis. Here we generate milligram quantities of oxidized human galectin-1 and undertake biophysical characterization. The protein adopts a number of different states. Two separable oxidized forms are identified that exist as largely mono-disperse solutions at higher milligram/ml concentrations. The presence of disulphide bonds is confirmed for these two protein forms, as is their change in overall shape and loss of lectin activity. Our studies lead to production of a particular mono-disperse oxidized human galectin-1 species that is anticipated most optimal for investigations requiring milligram/ml concentrations such as X-ray crystallography. © 2009 Bentham Science Publishers Ltd.

Publication Date


  • 2009

Citation


  • Scott, S. A., Bugarcic, A., & Blanchard, H. (2009). Characterisation of oxidized recombinant human Galectin-1. Protein and Peptide Letters, 16(10), 1249-1255. doi:10.2174/092986609789071342

Scopus Eid


  • 2-s2.0-69549097373

Start Page


  • 1249

End Page


  • 1255

Volume


  • 16

Issue


  • 10