Affinity chromatography of the chorismate mutase from Claviceps paspali based on specific interaction with the activator.
B. Sprossler,Franz Lingens +1 more
TLDR
The crude enzyme extract was partially purified by chromatography on DEAEcellulose and the chorismate mutase was eluted from the column with phosphate buffer supplemented with 103 M L-Trp.About:
This article is published in FEBS Letters.The article was published on 1970-02-16 and is currently open access. It has received 17 citations till now. The article focuses on the topics: Chorismate mutase.read more
Citations
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Journal ArticleDOI
The Purification of β-Galactosidase from Escherichia coli by Affinity Chromatography
TL;DR: The ability of the enzymatically inactive monomer forms to bind to the ligand column suggests that this affinity chromatographic method may be used in the purification of catalytically inactive mutant forms which retain the ability to bind substrate analogues.
Journal ArticleDOI
Interaction of human interferons with immobilized hydrophobic amino acids and dipeptides.
TL;DR: The interaction takes place under physiologic solvent conditions, thus revealing the high intrinsic hydrophobicity of both interferons, which cannot be displaced unless ethylene glycol is included in the eluant, indicating a hydrophobic interaction.
Book ChapterDOI
2 – Biospecific Affinity Chromatography and Related Methods
Jerker Porath,Tore Kristiansen +1 more
Book ChapterDOI
Chemically Reactive Derivatives of Polysaccharides
TL;DR: The chapter covers the production of all the known covalent derivatives of naturally occurringpolysaccharides, and discusses the reactions in which the polysaccharide chain is maintained largely, if not completely, intact.
References
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Journal ArticleDOI
Selective enzyme purification by affinity chromatography
TL;DR: The general principles and potential applications of "affinity chromatography," a protein purification technique that is indispensable to modern biological research, are explained.
Journal ArticleDOI
Spectrophotometric determination of microgram quantities of protein without nucleic acid interference
TL;DR: A spectrophotometric method which eliminates interference due to nucleic acid absorbance has been developed for determining protein concentration over the range of 5 to 180 μg/ml and the results obtained have been compared to those obtained with the Folin-Lowry and microbiuret methods.