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Chemical cross-linking immobilized concanavalin A for use in proteomic analyses.
- Source :
-
Preparative biochemistry & biotechnology [Prep Biochem Biotechnol] 2006; Vol. 36 (3), pp. 203-14. - Publication Year :
- 2006
-
Abstract
- Lectin affinity chromatography was used to reduce the amount of the abundant glycoprotein beta-conglycinin in total protein samples prepared from developing soybean (Glycine max L. Merrill cv. Jack) seeds. Electrophoretic analysis of both the concanavalin A-Sepharose binding and non-binding fraction revealed an abundant protein band at Mr 26,000. The amount of this protein was greatly increased when concanavalin A-Sepharose was used with urea-containing buffers. Peptide mass fingerprint analysis of this abundant protein band unequivocally identified it as concanavalin A (con A). A simple and gentle method was used to chemically cross-link the con A subunits so that the lectin-Sepharose retained the ability to bind high-mannose type glycoproteins. The chemically cross-linked con A-Sepharose was stable in buffers that contained up to 8M urea, making this an affinity matrix suitable for use in electrophoresis-based proteomic analyses.
Details
- Language :
- English
- ISSN :
- 1082-6068
- Volume :
- 36
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Preparative biochemistry & biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 16707331
- Full Text :
- https://doi.org/10.1080/10826060600716224