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Original Articles

A Long Acidic Domain Affects the Chromatographic Behaviour of a Neuronal Adaptor Protein on DEAE-Sepharose

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Pages 2048-2050 | Received 23 Apr 2003, Accepted 22 May 2003, Published online: 22 May 2014
 

Abstract

The stepwise chromatographic behaviour on DEAE-Sepharose of rat Fe65, a neuronal protein, was tested, using as eluants KCl, CaCl2, and MgCl2. Assays by western blot showed that Fe65 was eluted by CaCl2, at a ionic strength 20% lower than that of MgCl2 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.

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