Purification of plant complex protein extracts in non-denaturing conditions by in-solution isoelectric focusing

Anal Biochem. 2016 Sep 15:509:100-103. doi: 10.1016/j.ab.2016.07.004. Epub 2016 Jul 7.

Abstract

An alternative approach for plant complex protein extracts pre-purification by in-solution isoelectric focusing in non-denaturing conditions is presented. The separation of biologically active proteins, in narrow ranges of isoelectric point (pI) was obtained by a modified OFFGEL electrophoresis. Two different water-soluble protein extracts from Phragmites leaves were fractionated into 24 fractions within a 3-10 pI range at 10 °C in the absence of denaturing/reducing agents. One-dimensional electrophoretic analysis revealed different protein distribution patterns and the effective fractionation of both protein extracts. Peroxidase activity of each fraction confirmed that proteins remained active and pre-purification occurred. Biological triplicates assured the needed reproducibility.

Keywords: In-solution IEF; Non-denaturing conditions; OFFGEL electrophoresis; Phragmites sp.; Plant protein purification; pI.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Isoelectric Focusing / methods
  • Plant Extracts / chemistry*
  • Plant Leaves / chemistry*
  • Plant Proteins / chemistry*
  • Plant Proteins / isolation & purification*
  • Poaceae / chemistry*

Substances

  • Plant Extracts
  • Plant Proteins