Improved isoelectric focusing chromatography on strong anion exchange media via a new model that custom designs mobile phases using simple buffers
Article first published online: 25 OCT 2013
© 2013 Wiley Periodicals, Inc.
Biotechnology and Bioengineering
Volume 111, Issue 3, pages 552–564, March 2014
How to Cite
Choy, D. Y.C., Creagh, A. L. and Haynes, C. (2014), Improved isoelectric focusing chromatography on strong anion exchange media via a new model that custom designs mobile phases using simple buffers. Biotechnol. Bioeng., 111: 552–564. doi: 10.1002/bit.25122
- Issue published online: 21 JAN 2014
- Article first published online: 25 OCT 2013
- Accepted manuscript online: 25 SEP 2013 12:55AM EST
- Manuscript Accepted: 16 SEP 2013
- Manuscript Revised: 10 SEP 2013
- Manuscript Received: 2 AUG 2013
Additional supporting information may be found in the online version of this article at the publisher's web-site.
|bit25112-sm-0001-SupFig-S1.docx||439K||Figure S1. Isoelectric focusing (IEF) gel for 10 µL protein (10 mg mL−1) samples of myoglobin, carbonic anhydrase, conalbumin, bovine serum albumin, ovalbumin, β-amylase, trypsin inhibitor, β-lactoglobulin A, β-lactoglobulin B and α-lactalbumin (lanes 2–11). Samples were loaded onto a ReadyGel IEF gel pH 5–8 and electrophoresed in a Mini-Protean III unit. IEF protein standards (3 µL) containing cytochrome C (pI = 9.6), lentil lectin (pI's = 7.80, 8.00, and 8.20), human hemoglobulin C (pI = 7.5), human hemoglobulin A (pI = 7.1), equine myoglobin (pI's = 6.8 and 7.0), human carbonic anhydrase (pI = 6.5), bovine carbonic anhydrase (pI = 6.0), β-lactoglobulin B (pI = 5.1) and phycocyanin (pI's = 4.45, 4.65, and 4.75) were loaded to lanes 1 and 12 for reference.|
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