Positional reproducibility of protein spots in two-dimensional polyacrylamide gel electrophoresis using immobilised pH gradient isoelectric focusing in the first dimension: an interlaboratory comparison

Electrophoresis. 1994 Aug-Sep;15(8-9):1205-11. doi: 10.1002/elps.11501501182.

Abstract

An intra- and interlaboratory comparison of positional reproducibility of protein spots in two-dimensional electrophoresis using immobilised pH gradients (IPG) in the first dimension (IPG-DALT) was made. Aliquots of two different samples, human cardiac and barley leaf proteins, were separated in two different laboratories (London and Munich), using 180 mm long IPG gel strips, pH 4-8, for the first dimension and homogeneous SDS-PAGE gels (12% T) for the second dimension. Subsets of 340 (cardiac) and 200 (barley) well-resolved spots distributed across the 2-D gel patterns were selected for computer analysis (PDQUEST) of positional reproducibility. The IPG-dimension was highly reproducible in each laboratory, with a mean standard deviation of about 1 mm for both types of sample. Interlaboratory comparisons revealed identical results for barley with a mean standard deviation along the x-axis of about 1 mm, whereas the cardiac matchset showed slightly more variability (mean standard deviation approximately 1.5 mm). Nevertheless, IPG-DALT provides significantly improved reproducibility of spot positions compared to conventional isoelectric focusing with synthetic carrier ampholytes.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Electrophoresis, Gel, Two-Dimensional / methods
  • Electrophoresis, Gel, Two-Dimensional / standards*
  • Heart Ventricles
  • Hordeum / chemistry
  • Humans
  • Hydrogen-Ion Concentration
  • Indicators and Reagents
  • Isoelectric Focusing / methods
  • Isoelectric Focusing / standards*
  • Laboratories / standards*
  • Muscle Proteins / analysis
  • Muscle Proteins / isolation & purification
  • Myocardium / chemistry
  • Plant Leaves
  • Plant Proteins / analysis
  • Plant Proteins / isolation & purification
  • Proteins / analysis
  • Proteins / isolation & purification*
  • Reproducibility of Results
  • Software
  • Staining and Labeling

Substances

  • Indicators and Reagents
  • Muscle Proteins
  • Plant Proteins
  • Proteins