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Immobilized chymotrypsin by means of Schiff base copper(II) chelate.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1989 Jul 14; Vol. 162 (1), pp. 408-14. - Publication Year :
- 1989
-
Abstract
- A new method for cross-linking of protein was proposed in our previous work. The method is based on the spontaneous chelate formation process involving three components, salicylaldehyde moiety, alpha-amino acid residue and copper(II). In this paper versatility of the method as a purpose of immobilization of enzyme was described. Chymotrypsin-salicylaldehyde conjugate was immobilized to the agarose gel attached alpha-amino acid residue in the presence of copper(II) ion The enzyme was not eluted from the gel by washing with a copper free buffer though it was exclusively eluted by a medium containing EDTA. Catalytic activity of the chymotrypsin salicylaldehyde conjugate was not changed upon the immobilization. The method was proposed as a new tool for reversible immobilization of enzyme.
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 162
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 2751659
- Full Text :
- https://doi.org/10.1016/0006-291x(89)92012-3