Fundamentals of protein affinity chromatography: How to prepare and properly use an affinity matrix

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216275%3A25310%2F25%3A39923503" target="_blank" >RIV/00216275:25310/25:39923503 - isvavai.cz</a>

Výsledek na webu

<a href="https://doi.org/10.1016/j.chroma.2025.466061" target="_blank" >https://doi.org/10.1016/j.chroma.2025.466061</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.chroma.2025.466061" target="_blank" >10.1016/j.chroma.2025.466061</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Fundamentals of protein affinity chromatography: How to prepare and properly use an affinity matrix

Popis výsledku v původním jazyce

Affinity chromatography (AC) is a powerful method that relies on the principle of molecular recognition, exploiting the ability of various substances and biological compounds to form specific pairs, either reversibly or irreversibly. Attaching one reactive component to a solid-phase substrate allows the capture of a second interacting substance under mild conditions, even from the complex biological materials. When optimal elution conditions are adjusted, specifically captured molecules are quantitatively released from the affinity matrix, achieving them in a high purity. A well-designed affinity matrix combined with optimized separation conditions facilitates the acquisition of bioactive molecules in their native form. Given the wide range of substances suitable for affinity isolation, this article introduces the readers to the basics of protein AC, with the intention to provide a practical guide on how to prepare the affinity matrix and apply it for the effective isolation and purification of protein molecules.

Název v anglickém jazyce

Fundamentals of protein affinity chromatography: How to prepare and properly use an affinity matrix

Popis výsledku anglicky

Affinity chromatography (AC) is a powerful method that relies on the principle of molecular recognition, exploiting the ability of various substances and biological compounds to form specific pairs, either reversibly or irreversibly. Attaching one reactive component to a solid-phase substrate allows the capture of a second interacting substance under mild conditions, even from the complex biological materials. When optimal elution conditions are adjusted, specifically captured molecules are quantitatively released from the affinity matrix, achieving them in a high purity. A well-designed affinity matrix combined with optimized separation conditions facilitates the acquisition of bioactive molecules in their native form. Given the wide range of substances suitable for affinity isolation, this article introduces the readers to the basics of protein AC, with the intention to provide a practical guide on how to prepare the affinity matrix and apply it for the effective isolation and purification of protein molecules.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10400 - Chemical sciences

Projekt

<a href="/cs/project/EF17_048%2F0007421" target="_blank" >EF17_048/0007421: Posilování mezioborové spolupráce ve výzkumu nanomateriálů a při studiu jejich účinků na živé organismy</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2025

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Chromatography A

ISSN

0021-9673

e-ISSN

1873-3778

Svazek periodika

1756

Číslo periodika v rámci svazku

August 2025

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

28

Strana od-do

466061

Kód UT WoS článku

001504611800003

EID výsledku v databázi Scopus

2-s2.0-105006692458