Two-dimensional gel electrophoresis characterization of the mouse leukocyte proteome, using a tri-reagent for protein extraction

Nataliya I. Lenchik, Dominic M. Desiderio, Ivan Gerling

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The use of "tri-reagents" allows the concomitant isolation of DNA, RNA, and proteins for a complete molecular characterization of biological samples. The aim of the current study was to perform the comparative evaluation of two-dimensional gel proteomes isolated with or without a tri-reagent protein extraction step before dissolving the samples in the first-dimension electrophoresis buffer. We conclude that the use of trireagents increases the amount of protein extracted from the sample. Furthermore, an average of 301 ± 3.6 spots were found in gels from both sample preparation methods, whereas 71.7 ± 8.1 and 49.7 ± 2.3 spots were uniquely seen in tri-reagent and non-tri-reagent samples, respectively.

Original languageEnglish (US)
Pages (from-to)2202-2209
Number of pages8
JournalProteomics
Volume5
Issue number8
DOIs
StatePublished - May 1 2005

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Electrophoresis, Gel, Two-Dimensional
Proteome
Electrophoresis
Leukocytes
Gels
Proteins
Buffers
RNA
DNA

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

Cite this

Two-dimensional gel electrophoresis characterization of the mouse leukocyte proteome, using a tri-reagent for protein extraction. / Lenchik, Nataliya I.; Desiderio, Dominic M.; Gerling, Ivan.

In: Proteomics, Vol. 5, No. 8, 01.05.2005, p. 2202-2209.

Research output: Contribution to journalArticle

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