Coelectrophoresis of cardiac tissue from human, dog, rat and mouse: towards the establishment of an integrated two-dimensional protein database

Electrophoresis. 1995 Aug;16(8):1524-9. doi: 10.1002/elps.11501601252.


We have investigated the feasibility of identifying homologous proteins in whole tissue protein extracts of dog, mouse and rat hearts by comparison with our human heart two-dimensional (2-D) database. Samples of ventricular myocardial tissue from each of these species were coelectrophoresed with a human tissue sample. Gels were silver stained and patterns were analysed using PDQUEST. The number of proteins comigrating with human proteins was 301, 201 and 356 for the dog, mouse and rat, respectively. In the dog pattern, 33 of these comigrating proteins were tentatively identified from the similarity between their migration properties and those of known human proteins. Twenty-nine such proteins were identified in the mouse pattern while 30 comigrating rat proteins were identified. While these tentative identifications require confirmation, we feel that this technique offers a useful shortcut in the characterisation of proteins present in similar tissue samples from different species and avoids the necessity for duplicating laborious procedures, such as protein microsequencing, otherwise used in the identification of these proteins in each species.

MeSH terms

  • Animals
  • Databases, Factual*
  • Dogs
  • Electrophoresis, Gel, Two-Dimensional / methods*
  • Electrophoresis, Polyacrylamide Gel
  • Heart Ventricles / chemistry
  • Humans
  • Isoelectric Focusing
  • Isoelectric Point
  • Mice
  • Myocardium / chemistry*
  • Proteins / analysis*
  • Rats
  • Silver Staining


  • Proteins