An immunoaffinity purification method for the proteomic analysis of ubiquitinated protein complexes

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Proteomic analysis of ubiquitinated proteins from human MCF-7 breast cancer cells by immunoaffinity purification and mass spectrometry.

Post-translational modification of proteins via the covalent attachment of Ubiquitin (Ub) plays an important role in the regulation of protein stability and function in eukaryotic cells. In the present study, we describe a novel method for identifying ubiquitinated proteins from a complex biological sample, such as a whole cell lysate, using a combination of immunoaffinity purification and liqu...

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[10] Protein- and Immunoaffinity Purification of Multiprotein Complexes

We have not had any problems using this method to purify proteins that are lethal on overexpression, including Abplp and Duolp. Although cells are dying during the induction, significant amounts of recombinant protein are produced. Because some proteins are sensitive to longer (>4 hr) induction times, it may be important to test protein expression at different time points during the induction. ...

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Development of an Immunoaffinity Method for Purification of Streptokinase

BACKGROUND Streptokinase is a potent activator of plasminogen to plasmin, the enzyme that can solubilize the fibrin network in blood clots. Streptokinase is currently used in clinical medicine as a thrombolytic agent. It is naturally secreted by β-hemolytic streptococci. METHODS To reach an efficient method of purification, an immunoaffinity chromatography method was developed that could puri...

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ژورنال

عنوان ژورنال: Analytical Biochemistry

سال: 2013

ISSN: 0003-2697

DOI: 10.1016/j.ab.2013.05.020