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Immunoaffinity chromatography of diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase from Saccharomyces cerevisiae.
- Source :
-
Biotechnology and applied biochemistry [Biotechnol Appl Biochem] 1990 Jun; Vol. 12 (3), pp. 276-83. - Publication Year :
- 1990
-
Abstract
- Diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) phosphorylase has been isolated previously using classical protein isolation techniques [A. Guranowski and S. Blanquet (1985) J. Biol. Chem. 260, 3542-3547]. A protein A-Sepharose immunoaffinity column was prepared to simplify the purification procedure. The immunoaffinity column was prepared using specific polyclonal antibodies to Ap4A phosphorylase covalently coupled to protein A-Sepharose with dimethyl pimelimidate by a modification of the procedure of C. Schneider et al. [(1982) J. Biol. Chem. 257, 10,766-10,769]. The specific activity of the immunoaffinity-purified enzyme showed an increase equivalent to the specific activity obtained by chromatography on DEAE-cellulose and hydroxyapatite columns.
Details
- Language :
- English
- ISSN :
- 0885-4513
- Volume :
- 12
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biotechnology and applied biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 2163260