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Article Dans Une Revue Electrophoresis Année : 2000

Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins

Résumé

As a complementary approach to genome projects, proteomic analyses have been set up to identify new gene products. One of the major challenges in proteomics concerns membrane proteins, especially the minor ones. A procedure based on the differential extraction of membrane proteins in chloroform/methanol mixtures, was tested on the two different chloroplast membrane systems: envolope and thylakoid membranes. Combining the use of classical sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and mass spectrometry analyses, this procedure enabled identification of hydrophobic proteins. The propensity of hydrophobic proteins to partition in chloroform/methanol mixtures was directly correlated with the number of amino acid residues/number of putative transmembrane regions (Res/TM ratio). Regardless of the particular case of some lipid-interacting proteins, chloroform/methanol extractions allowed enrichment of hydrophobic proteins and exclusion of hydrophilic proteins from both membrane systems, thus demonstrating the versatility of the procedure.

Dates et versions

hal-04495836 , version 1 (08-03-2024)

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Myriam Ferro, Daphné Seigneurin-Berny, Norbert Rolland, Agnès Chapel, Daniel Salvi, et al.. Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins. Electrophoresis, 2000, 21 (16), pp.3517-3526. ⟨10.1002/1522-2683(20001001)21:16<3517::AID-ELPS3517>3.0.CO;2-H⟩. ⟨hal-04495836⟩
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