Large scale preparation and purification of apo-D-aminoacid oxidase for use in novel amplification assays

Autor:	Brian R. Rabin, Mark Fisher, Stuart Harbron
Rok vydání:	1992
Předmět:	chemistry.chemical_classification Oxidase test Chromatography Ion exchange Chemistry Phosphatase Size-exclusion chromatography D-amino acid oxidase Applied Microbiology and Biotechnology Biochemistry Diafiltration Enzyme Nucleotidase
Zdroj:	Biotechnology Techniques. 6:55-60
ISSN:	1573-6784 0951-208X
DOI:	10.1007/bf02438689
Popis:	Dissociation of FAD from D-aminoacid oxidase occurred most rapidly at pH 6.0 in the presence of 1 M KBr. Diafiltration of 0.6 g of enzyme under these conditions yielded apoenzyme containing 1.3% of residual holoenzyme activity, which was subsequently reduced to less than 0.01% by chromatography on Blue Sepharose and ion exchange, giving material containing
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::8aca8d7f5d86e92c89e953bef49bbf0b https://doi.org/10.1007/bf02438689 Zobrazit plný text záznamu Full text from SpringerLink