Spinach nitrate reductase: Further purification and removal of ‘nicked’ sub-units by affinity chromatography

Autor:	R.J. Fido, B.A. Notton
Rok vydání:	1984
Předmět:	chemistry.chemical_classification Gel electrophoresis Chromatography biology Soil Science Hydroxylapatite Reductase Nitrate reductase biology.organism_classification chemistry.chemical_compound Enzyme chemistry Affinity chromatography Spinach Specific activity Agronomy and Crop Science
Zdroj:	Plant Science Letters. 37:87-91
ISSN:	0304-4211
DOI:	10.1016/0304-4211(84)90208-6
Popis:	NADH-nitrate reductase (EC 1.6.6.1) from spinach (Spinacea oleracea L. v. Noorman) has been purified 3400-fold by a multi-stage procedure involving streptomycin sulphate, (NH4)2SO4, hydroxylapatite, molecular seiving and two stages of affinity chromatography using blue-Sepharose and 5′ AMP-Sepharose. The enzyme has a specific activity of 51 μmol NO2− produced min−1 mg−1 and a functional haem with extinction coefficients (mM) of 127 at 412 nm (oxidized) and 172 at 423 (NADH-reduced). Gel electrophoresis indicates two sub-units of approx. 110 000 and 120 000.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::08a1930596c0348751fc5df29a738175 https://doi.org/10.1016/0304-4211(84)90208-6 Zobrazit plný text záznamu