Analysis of nickel-binding peptides in a human hepidermoid cancer cell line by Ni-NTA affinity chromatography and mass spectrometry

Lamberti, A; Sanges, C; Longo, O; Chambery, Angela; DI MARO, Antimo; Parente, A; Masullo, M; Arcari, P.

doi:10.2174/092986608786071157

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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. © 2008 Bentham Science Publishers Ltd.

Titolo:	Analysis of nickel-binding peptides in a human hepidermoid cancer cell line by Ni-NTA affinity chromatography and mass spectrometry
Autori:	LAMBERTI A SANGES C LONGO O CHAMBERY, Angela DI MARO, Antimo PARENTE A MASULLO M ARCARI P. mostra contributor esterni nascondi contributor esterni
Data di pubblicazione:	2008
Rivista:	PROTEIN AND PEPTIDE LETTERS
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. © 2008 Bentham Science Publishers Ltd.
Handle:	http://hdl.handle.net/11591/190215
Appare nelle tipologie:	1.1 Articolo in rivista

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