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Removal of Sodium Dodecyl Sulfate from Protein Samples Prior to Matrix-assisted Laser Desorption/ionization Mass Spectrometry by Maja Puchades; Ann Westman; Kaj Blennow; Pia Davidsson is a Chemistry article available to read on EtoBox.

What is Removal of Sodium Dodecyl Sulfate from Protein Samples Prior to Matrix-assisted Laser Desorption/ionization Mass Spectrometry about?

Sodium dodecyl sulfate (SDS) is widely used for protein solubilization and for separation of proteins by SDS polyacrylamide gel electrophoresis (SDS-PAGE). However, SDS interferes with other techniques used for characterization of proteins, such as mass spectrometry (MS) and amino acid sequencing. In this paper, we have compared three procedures to remove SDS from proteins, including chloroform/methanol/water extraction (C/M/W), cold acetone extraction and desalting columns, in order to find a rapid and reproducible procedure that provides sufficient reduction of SDS and high recovery rates for proteins prior to matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS). A 1000fold reduction of SDS concentration and a protein recovery at approximately 50% were obtained with the C/M/W procedure. The cold acetone procedure gave a 100-fold reduction of SDS and a protein recovery of approximately 80%. By using desalting columns, the removal of SDS was 100-fold, with a protein recovery of nearly 50%. Both the C/M/W and the cold acetone methods provided sufficient reduction of SDS, high recovery rates of protein and allowed the acquisition of MALDI spectra

Who reads Removal of Sodium Dodecyl Sulfate from Protein Samples Prior to Matrix-assisted Laser Desorption/ionization Mass Spectrometry?

It is typically read by researchers, students, and practitioners in Chemistry.

Author
Maja Puchades; Ann Westman; Kaj Blennow; Pia Davidsson
Publisher
John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0951-4198)
Published
1999
Language
EN
Field
Chemistry (Physical Sciences)

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