A stable, high capacity, F-actin affinity column.
نویسندگان
چکیده
منابع مشابه
A human β-III-spectrin spinocerebellar ataxia type 5 mutation causes high-affinity F-actin binding.
Spinocerebellar ataxia type 5 (SCA5) is a human neurodegenerative disease that stems from mutations in the SPTBN2 gene encoding the protein β-III-spectrin. Here we investigated the molecular consequence of a SCA5 missense mutation that results in a L253P substitution in the actin-binding domain (ABD) of β-III-spectrin. We report that the L253P substitution in the isolated β-III-spectrin ABD cau...
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We have developed stable and easy to use filamentous actin (F-actin) affinity-chromatography columns that selectively purify proteins that bind to actin filaments from cell extracts. Most traditional assays for actin-associated proteins screen for their effects on actin polymerization or actin filament crosslinking. Because our technique requires only actin-filament binding, it can identify add...
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One simple structural change in compound (I), the destruction of its symmetry by its conversion into n-propyl-2-pyridyl disulphide [III, R = C3H7(propyl)-S-S-2-Py], has permitted the demonstration of an important property of the thiol proteinases, the existence of nucleophilic character in the uninterrupted thiol-imidazole interactive systems of their active centres. The reactions of 2-Py-S-S-2...
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Regulated expression of proteins involved in mammalian iron metabolism is achieved in part through the interaction of the iron regulatory proteins IRP1 and IRP2 with highly conserved RNA stem-loop structures, known as iron-responsive elements (IREs), that are located within the 5' or 3' untranslated regions of regulated transcripts. As part of an effort to determine the structures of the IRP-IR...
متن کاملDecavanadate binding to a high affinity site near the myosin catalytic centre inhibits F-actin-stimulated myosin ATPase activity.
Decameric vanadate (V(10)) inhibits the actin-stimulated myosin ATPase activity, noncompetitively with actin or with ATP upon interaction with a high-affinity binding site (K(i) = 0.27 +/- 0.05 microM) in myosin subfragment-1 (S1). The binding of V(10) to S1 can be monitored from titration with V(10) of the fluorescence of S1 labeled at Cys-707 and Cys-697 with N-iodo-acetyl-N'-(5-sulfo-1-napht...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)33627-5