Schiff base copper(II) chelate as a tool for immobilization of protein.

Publisher Website
Google Scholar
Abstract
In our previous report a new methodolgoy for intermolecular cross-linking or bridging of protein utilizing a spontaneous chelate formation process was proposed. In this paper the reliability of the process as a tool for protein immobilization has been further evaluated. The chromatographic behavior of tryptophan in a column packed with Sepharose coupled iwht salicylaldehyde residue showed that the .alpha.-amino acid was boud tightly to the gel in the presence of copper (II) ion and was eluted by the addition of ethylenediaminetetraacetate (EDTA). It was also proved that subtilisin modified with an .alpha.-amino acid residue was immobilized on the column, and this binding was reversed by the addition of EDTA as well.

This publication has 1 reference indexed in Scilit: