Trending Affinity Chromatography-linked topics for 7 of August 2019

This site features trending Affinity Chromatography-linked items from the web for 7 of August 2019.

Trending Affinity Chromatography news item:

New reports size up the Boronate Affinity Chromatography market: Affinity chromatography is a separation method that utilizes the specific binding interaction between an immobilized ligand and its binding partner for separation and purification. Boronate affinity chromatography is based on the boronate functional group and used for the selective separation and molecular recognition of cis-diol-containing compounds in industries like healthcare, pharmaceutical, and biotechnology. Scope of the Report: This report studies the Boronate Affinity Chromatography market status and outlook of Global and major regions, from angles of players, countries, product types and end industries; this report analyzes the top players in global market, and splits the Boronate Affinity Chromatography market by product type and applications/end industries… read the entire news item (from PR News Globe)

Featured recent scientific publication on Affinity Chromatography:

Plasma protein binding of dietary polyphenols to human serum albumin: A high performance affinity chromatography approach: Herein, the protein binding rates of structurally different flavonoids to human serum albumin (HSA) were elucidated by applying the high performance affinity chromatography (HPAC). The flavonoids with hydroxyl groups on ring A showed a higher protein binding rate compared with those that there was no hydroxyl on ring A. However, the hydroxylation of ring B lowered the protein binding rate. It was also found that an additional methoxy group in flavone ring A would decrease the protein binding rate. Nevertheless, the methoxy group in flavanone ring A (position 6) and isoflavone ring B (position 4′) increased the protein binding rate. Methoxy group at other positions of flavonoids slightly enhanced or no significantly affected the binding rates on human serum albumin. Hydrogenation of C2C3 double bond of flavonoids decreased the protein binding rate and had the same effect as glycosylation which decrease the protein binding rate by 5%-25%… read the entire scientific publication (from Food Chemistry)

Trending tweet on #affinitychromatography:



Background knowledge on Affinity Chromatography:

Affinity chromatography (AC) is a variant of liquid chromatography in which biospecific and reversible interactions between biologically active or structurally unique and complementary molecules are used for the selective extraction, separation, purification, analysis, or tagging of specific macromolecules or cell components from crude biological samples. AC was first introduced as a procedure for purifying enzymes and proteins more than 30 years ago. AC is based on the principles of molecular recognition, and today it is one of the most powerful techniques available for purifying physiologically or structurally interacting proteins. In addition to the multitude of proteins purified by AC, the method has also been an indispensable tool for studying many biological processes, such as the mechanism of action of enzymes and hormones, protein–protein or cell–cell interactions, and others encountered in genetic engineering. The emergence of many related methodologies, which are based on molecular recognition (or biorecognition), has impacted virtually all fields of research in the biological sciences. The Key Steps in AC: The first step involves the preparation of a matrix support (resin) material to which a unique “ligand” (typically a small molecule such as an enzyme inhibitor or substrate) is attached (coupled) irreversibly. This is accomplished by chemical activation of the inert resin followed by the irreversible attachment of the ligand (Figure 1). Such a derivatized resin is then used for purification of a biologically active compound by AC following a three-step process as illustrated in Figure 2. These steps are (1) adsorption or reversible attachment of the protein (or macromolecule) to be purified from the mixture to the resin, (2) thorough washing of this resin, and (3) then elution or removal of the protein from the resin. Generally, the used resin can be thoroughly washed and cleaned (regenerated) and used again for the same purpose. Why and Where AC Works: Biological macromolecules such as enzymes, polynucleotides (like DNA and RNA), antibodies, receptors, and structural proteins normally interact with chemically different but highly specific molecules by virtue of conformationally unique active sites (such as in enzymes, for substrate binding and catalysis) or binding recognition sites (as for antigens, hormones, and oligonucleotides). If one of these partners of the interacting pair (e.g., enzyme inhibitor) is immobilized on a polymeric carrier, it can be used to attract and isolate the complementary partner (e.g., the enzyme) by simply passing a cell extract containing the latter through a chromatography column packed with the immobilized molecule. Molecules without appreciable affinity for the immobilized ligand will pass unretarded through the column, whereas those capable of binding to the ligand will be retained (adsorbed)… read more (from Encyclopedia of Biological Chemistry, 1st Edition)

Keywords: Affinity Chromatography, #affinitychromatography, molecular recognition (biorecognition), high performance affinity chromatography (HPAC), human serum albumin (HSA), flavonoids, boronate affinity chromatography.

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