Protein Purification Using PDZ Affinity Chromatography
نویسندگان
چکیده
منابع مشابه
Protein purification using PDZ affinity chromatography.
PDZ domains function in nature as protein-binding domains within scaffold and membrane-associated proteins. They comprise approximately 90 residues and undergo specific, high-affinity interactions with complementary C-terminal peptide sequences, other PDZ domains, and/or phospholipids. We have previously shown that the specific, strong interactions of PDZ domains with their ligands make them we...
متن کاملProtein Purification by Affinity Chromatography
The preparation of a number of agarose and polyacrylamide bead derivatives useful in the purification of proteins by afhnity chromatography is described. These techniques permit (a) the attachment of ligands to the gel through extended hydrocarbon chains which place the ligand at varying distances from the gel matrix backbone; (b) the covalent attachment of ligands to agarose or polyacrylamide ...
متن کاملProtein Purification by Affinity Chromatography
The preparation of a number of agarose and polyacrylamide bead derivatives useful in the purification of proteins by afhnity chromatography is described. These techniques permit (a) the attachment of ligands to the gel through extended hydrocarbon chains which place the ligand at varying distances from the gel matrix backbone; (b) the covalent attachment of ligands to agarose or polyacrylamide ...
متن کاملProtein Purification by Affinity Chromatography
Affinity chromatography is a method which depends essentially on the interaction between the molecule to be purified and a solid phase that will allow the separation of contaminants. Lectins are carbohydrate-binding proteins which can be purified by affinity chromatography; also, the presence of multiple molecular forms of lectins in a preparation can be separated. Immobilized lectins have been...
متن کاملProtein Purification by Affinity Chromatography
The preparation of a number of agarose and polyacrylamide bead derivatives useful in the purification of proteins by afhnity chromatography is described. These techniques permit (a) the attachment of ligands to the gel through extended hydrocarbon chains which place the ligand at varying distances from the gel matrix backbone; (b) the covalent attachment of ligands to agarose or polyacrylamide ...
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ژورنال
عنوان ژورنال: Current Protocols in Protein Science
سال: 2015
ISSN: 1934-3655,1934-3663
DOI: 10.1002/0471140864.ps0910s80