Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients

Details Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients

2006-12-04

arxiv.org/abs/q-bio/0612002v1

Electrophoresis 18 (31/03/1997) 307-16

Biology

Quantitative Biology

Genomics

website publisher: http://www.interscience.wiley.com

Scientific paper

10.1002/elps.1150180303

Membrane and nuclear proteins of poor solubility have been separated by high resolution two-dimensional (2-D) gel electrophoresis. Isoelectric focusing with immobilized pH gradients leads to severe quantitative losses of proteins in the resulting 2-D map, although the resolution is usually high. Protein solubility could be improved by using denaturing solutions containing various detergents and chaotropes. Best results were obtained with a denaturing solution containing urea, thiourea, and detergents (both nonionic and zwitterionic). The usefulness of thiourea-containing denaturing mixtures is shown for microsomal and nuclear proteins as well as for tubulin, a protein highly prone to aggregation.

Affiliated with

Also associated with

No associations

Rating

Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Improvement of the solubilization of proteins in two-dimensional electrophoresis with immobilized pH gradients will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-649698