Displacement affinity chromatography of protein phosphatase one (PP1) complexes
نویسندگان
چکیده
منابع مشابه
Preparation of Plasminogen by Affinity Chromatography
Background: Plasminogen is one of the compounds derived from human plasma. Activation of plasminogen produces plasmin. Plasmin is able to lyse fibrinogen, fibrin, and some other human plasma proteins. The aim of the present work was to study the separation of human plasminogen by affinity chromatography using gel lysine Sepharose. Materials and Methods: Normal human plasma was used as the...
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The deletion of the protein phosphatase-1 (PP1) regulator known as Nuclear Inhibitor of PP1 (NIPP1) is embryonic lethal during gastrulation, hinting at a key role of PP1-NIPP1 in lineage specification. Consistent with this notion we show here that a mild, stable overexpression of NIPP1 in HeLa cells caused a massive induction of genes of the mesenchymal lineage, in particular smooth/cardiac-mus...
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 ...
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We have analyzed the nature of RecA protein-RecA protein interactions using an affinity column prepared by coupling RecA protein to an agarose support. When radiolabeled soluble proteins from Escherichia coli are applied to this column, only the labeled RecA protein from the extract was selectively retained and bound tightly to the affinity column. Efficient binding of purified 35S-labeled RecA...
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ژورنال
عنوان ژورنال: BMC Biochemistry
سال: 2008
ISSN: 1471-2091
DOI: 10.1186/1471-2091-9-28