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

Analytical Biochemistry

Journal Article

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. © 2016

Publication

Year of publication: 2016

Identifiers

ISSN: 00032697

Locators

DOI: 10.1016/j.ab.2016.07.004

Alternative Titles