Abstract
To elucidate whether eukaryotic elongation factor 1A (eEF-1A) in a human hepidermoid cancer cell line (H1355) belonged to the family of the Ni-interacting protein, we analyzed the sequence of peptides obtained by on-Ni- NTA-agarose tryptic digestion of proteins from H1355 cell extract. LC/MS analysis showed the presence of several peptides mainly from abundant cellular proteins corresponding to eEF-1A, tubulin and actin. The results indicated that F-actin strongly binds to Ni-NTA-agarose whereas the other proteins are indirectly bound to the resin because of the formation of a protein-protein complex with actin.
Keywords: Affinity chromatography, nickel-binding protein, tandem mass spectrometry, actin, tubulin, elongation factor 1A
Protein & Peptide Letters
Title: Analysis of Nickel-Binding Peptides in a Human Hepidermoid Cancer Cell Line by Ni-NTA Affinity Chromatography and Mass Spectrometry
Volume: 15 Issue: 10
Author(s): Annalisa Lamberti, Carmen Sanges, Olimpia Longo, Angela Chambery, Antimo Di Maro, Augusto Parente, Mariorosario Masullo and Paolo Arcari
Affiliation:
Keywords: Affinity chromatography, nickel-binding protein, tandem mass spectrometry, actin, tubulin, elongation factor 1A
Abstract: To elucidate whether eukaryotic elongation factor 1A (eEF-1A) in a human hepidermoid cancer cell line (H1355) belonged to the family of the Ni-interacting protein, we analyzed the sequence of peptides obtained by on-Ni- NTA-agarose tryptic digestion of proteins from H1355 cell extract. LC/MS analysis showed the presence of several peptides mainly from abundant cellular proteins corresponding to eEF-1A, tubulin and actin. The results indicated that F-actin strongly binds to Ni-NTA-agarose whereas the other proteins are indirectly bound to the resin because of the formation of a protein-protein complex with actin.
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Lamberti Annalisa, Sanges Carmen, Longo Olimpia, Chambery Angela, Maro Di Antimo, Parente Augusto, Masullo Mariorosario and Arcari Paolo, Analysis of Nickel-Binding Peptides in a Human Hepidermoid Cancer Cell Line by Ni-NTA Affinity Chromatography and Mass Spectrometry, Protein & Peptide Letters 2008; 15 (10) . https://dx.doi.org/10.2174/092986608786071157
DOI https://dx.doi.org/10.2174/092986608786071157 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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