Complex Hydride Purification

Complex hydride purification is the isolation of a chemically defined metal hydride containing a molecular anion, such as a borohydride or aluminate, from synthesis mixtures and unwanted contaminants. The process exploits differences in solubility, phase behavior, reactivity, and thermal stability, often through selective dissolution, filtration, washing, recrystallization, and controlled drying under an inert atmosphere. Effective purification limits residual salts, unreacted reagents, solvent, and decomposition products that can alter hydride composition and performance. In chemistry, purified complex hydrides support reliable studies of hydrogen storage, chemical reduction, ionic conductivity, and solid-state transformations while improving reproducibility and safety in handling air- or moisture-sensitive materials.

Complex Hydride Purification - Related Videos

Research

JoVE Journal - Biochemistry

Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells

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Cited by 7 •

2017

We describe here a novel, robust, and efficient tandem affinity purification (TAP) method for the expression, isolation, and characterization of protein complexes from eukaryotic cells. This protocol could be utilized for the biochemical characterization of discrete complexes as well as the identification of novel interactors and post-translational modifications that regulate their function.

Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes

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Cited by 8 •

2009

The genome of the influenza A virus consists of eight separate complexes of RNA and proteins, termed viral ribonucleoprotein complexes (vRNPs). This paper describes the glycerol gradient purification and transmission electron microscopy visualization of influenza A vRNPs.

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method

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Cited by 4 •

2016

The Tandem Affinity Purification (TAP) method has been used extensively to isolate native complexes from cellular extract, primarily eukaryotic, for proteomics. Here, we present a TAP method protocol optimized for purification of native complexes for structural studies.

Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes

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Cited by 7 •

2014

This protocol describes a procedure for generating and purifying wild type and mutant versions of the human INO80 chromatin remodeling complex. Epitope tagged versions of INO80 subunits are stably expressed in HEK293 cells, and complete complexes and complexes lacking specific sets of subunits are purified by immunoaffinity chromatography.

Research

JoVE Journal - Biochemistry
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Purification and Quality Control of Recombinant Septin Complexes for Cell-Free Reconstitution

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Cited by 2 •

2022

In vitro reconstitution of cytoskeletal proteins is a vital tool to understand the basic functional properties of these proteins. The present paper describes a protocol to purify and assess the quality of recombinant septin complexes, which play a central role in cell division and migration.

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