NADP+-specific isocitrate dehydrogenase of Excherichia coli. III. Two-step purification employing affinity chromatography

Autor:	M, Hy, H C, Reeves
Rok vydání:	1976
Předmět:	Escherichia coli Chromatography Affinity Isocitrate Dehydrogenase NADP
Zdroj:	Biochimica et biophysica acta. 445(2)
ISSN:	0006-3002
Popis:	The NADP+-specific isocitrate dehydrogenase (threo-DS-isocitrate:NADP+ oxidoreductase (decarboxylating), EC 1.1.1.42) of Excherichia coli has been purified to electrophoretic homogeneity by a two-step purification procedure employing affinity chromatography. The overall yield of enzyme was 30% with specific activity 125 mumol/min per ng protein. Electrophoretic homogeneity of the isocitrate dehydrogenase was deterimed in analytical polyacrylamide gels in a Tris/acetate/EDTA buffer system at pH 7.5 and in a citrate/phosphate buffer system at pH 6.0.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::f1de5100906f31712aaa5166689bfdf4 https://pubmed.ncbi.nlm.nih.gov/8141 Zobrazit plný text záznamu