Affinity purification ofHydraglutathione binding proteins
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چکیده
منابع مشابه
Purification of sequence-specific DNA-binding proteins by affinity chromatography.
The affinity chromatography procedure described in this unit uses DNA containing specific recognition sites for the desired protein that has been covalently linked to a solid support. Preparation of a DNA affinity resin, including cyanogen bromide (CNBr) activation of the agarose support, is described, and an alternate protocol provides a method to couple DNA to commercially available CNBr-acti...
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Background: Protein purification is the most complicated issue in the downstream processes of recombinant protein production; therefore, improved selective purification methods are important. Affinity-based protein purification method using His-tag and Ni-NTA resins is one of the most common strategies. MNPs can be used as a beneficial alternative for Ni-NTA resins. However, there is no data on...
متن کاملIdentifying mRNAs bound by RNA-binding proteins using affinity purification and differential display.
Many methods are available and widely used to determine specific proteins that bind to a particular RNA of interest. However, approaches to identify unknown substrate RNAs to which an RNA-binding protein binds and potentially regulates are not as common. In this article we describe a technique termed isolation of specific nucleic acids associated with proteins (SNAAP) that allows the identifica...
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Characterization of proteins binding to the promoters of eukaryotic genes has proved essential for understanding the transcriptional regulation of viral and cellular genes. Because of the low abundance of these proteins in the cell, conventional purification of these molecules has been laborious. In contrast, sequencespecific DNA affinity chromatography has greatly faciliated rapid isolation an...
متن کاملAffinity purification of Alu-DNA-repeat-binding proteins from human somatic cells.
A 66-kD Alu-DNA-repeat binding protein was identified in human somatic cell nucleoplasm. Gel shift assay, southwestern blotting, and affinity purification on DNA attached to a carrier were used. A 60-kD protein copurified with the 66-kD protein during affinity purification, probably due to protein--protein interactions. The gel shift assay reveals multiple complexes with exponential dependence ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1994
ISSN: 0014-5793
DOI: 10.1016/0014-5793(94)01154-0