High-Resolution Two-Dimensional Electrophoresis of Bovine Caseins

Michael G. Zeece, Douglas L. Holt, Randy L. Wehling, Michael B. Liewen, Lynne R. Bush

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Abstract

This work describes a high-resolution two-dimensional electrophoretic method for identification of bovine milk caseins. The isoelectric focusing separation was carried out in 100-jtL capillary tubes using high field strengths to achieve enhanced resolution. Subsequent sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was performed in a minigel format, and the result of the combined techniques gave enhanced protein resolution while requiring substantially less time than conventional two-dimensional methods. The procedure readily distinguished various isoforms of caseins, as well as phosphorylated forms of the proteins. The method was also used to demonstrate the effect of a proteinase derived from a Pseudomonas species on milk proteins.

Original languageEnglish (US)
Pages (from-to)378-383
Number of pages6
JournalJournal of Agricultural and Food Chemistry
Volume37
Issue number2
DOIs
StatePublished - Mar 1 1989

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ASJC Scopus subject areas

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

Cite this

Zeece, M. G., Holt, D. L., Wehling, R. L., Liewen, M. B., & Bush, L. R. (1989). High-Resolution Two-Dimensional Electrophoresis of Bovine Caseins. Journal of Agricultural and Food Chemistry, 37(2), 378-383. https://doi.org/10.1021/jf00086a023