Immunoaffinity chromatography of diadenosine 5',5''-P1,P4-tetraphosphate phosphorylase from Saccharomyces cerevisiae

Autor:	D M, Avila, V, Kaushal, L D, Barnes
Rok vydání:	1990
Předmět:	Evaluation Studies as Topic Sepharose Saccharomyces cerevisiae Nucleotidyltransferases Chromatography Affinity Biotechnology
Zdroj:	Biotechnology and applied biochemistry. 12(3)
ISSN:	0885-4513
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::64b1f13209dbe138b7e2724e0fa53ba5 https://pubmed.ncbi.nlm.nih.gov/2163260 Zobrazit plný text záznamu Plný text