Analysis of Nickel-Binding Peptides in a Human Hepidermoid Cancer Cell Line by Ni-NTA Affinity Chromatography and Mass Spectrometry

Author(s): Annalisa Lamberti, Carmen Sanges, Olimpia Longo, Angela Chambery, Antimo Di Maro, Augusto Parente, Mariorosario Masullo, Paolo Arcari

Journal Name: Protein & Peptide Letters

Volume 15 , Issue 10 , 2008

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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

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Article Details

Year: 2008
Page: [1126 - 1131]
Pages: 6
DOI: 10.2174/092986608786071157
Price: $65

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