A Long Acidic Domain Affects the Chromatographic Behaviour of a Neuronal Adaptor Protein on DEAE-Sepharose(Biochemistry & Molecular Biology)
スポンサーリンク
概要
- 論文の詳細を見る
The stepwise chromatographic behaviour on DEAE-Sepharose of rat Fe65, a neuronal protein, was tested, using as eluants KCl, CaCl_2, and MgCl_2. Assays by western blot showed that Fe65 was eluted by CaCl_2, at a ionic strength 20% lower than that of MgCl_2 or KCl. Interestingly, in the case of a truncated Fe65, lacking a glutamic acid rich region at the N-terminus, the ionic strengths of the various eluants were almost identical. These results suggested a possible inhibitory role of calcium ions in the binding of the protein to DEAE and a specific affinity of these ions for long acidic stretches.
- 社団法人日本農芸化学会の論文
- 2003-09-23
著者
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Zambrano Nicola
Dipartimento Di Biochimica E Biotecnologie Mediche Universita Di Napoli Federico Ii
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Longo Olimpia
Dipartimento Di Biochimica E Biotecnologie Mediche Universita Di Napoli Federico Ii
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Arcari Paolo
Dipartimento Di Biochimica E Biotecnologie Mediche Universita Di Napoli Federico Ii
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Lamberti Annalisa
Dipartimento Di Biochimica E Biotecnologie Mediche Universita Di Napoli Federico Ii
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LONGO Olimpia
Department of Biochemistry and Medical Biotechnologies, University of Naples Federico II
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LAMBERTI Annalisa
Department of Biochemistry and Medical Biotechnologies, University of Naples Federico II
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ZAMBRANO Nicola
Department of Biochemistry and Medical Biotechnologies, University of Naples Federico II
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ARCARI Paolo
Department of Biochemistry and Medical Biotechnologies, University of Naples Federico II
関連論文
- Probing the Secondary Structure of a Recombinant Neuronal Adaptor Protein and Its Phosphotyrosine Binding Domains
- A Long Acidic Domain Affects the Chromatographic Behaviour of a Neuronal Adaptor Protein on DEAE-Sepharose(Biochemistry & Molecular Biology)