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090			_aB-5828
245	1	0	_aExploring affinity chromatography in proteomics: A comprehensive review
490	0		_aAnalytica Chimica Acta, 1306, p.342513, 2024
500			_aArtículo
520	3		_aOver the past decades, the proteomics field has undergone rapid growth. Progress in mass spectrometry and bioinformatics, together with separation methods, has brought many innovative approaches to the study of the molecular biology of the cell. The potential of affinity chromatography was recognized immediately after its first application in proteomics, and since that time, it has become one of the cornerstones of many proteomic protocols. Indeed, this chromatographic technique exploiting the specific binding between two molecules has been employed for numerous purposes, from selective removal of interfering (over)abundant proteins or enrichment of scarce biomarkers in complex biological samples to mapping the post-translational modifications and protein interactions with other proteins, nucleic acids or biologically active small molecules. This review presents a comprehensive survey of this versatile analytical tool in current proteomics. To navigate the reader, the haphazard space of affinity separations is classified according to the experiment's aims and the separated molecule's nature. Different types of available ligands and experimental strategies are discussed in further detail for each of the mentioned procedures.
650	1	4	_aAFFINITY CHROMATOGRAPHY
650	1	4	_aAFFINITY DEPLETION
650	1	4	_aAFFINITY ENRICHMENT
650	1	4	_aMASS SPECTROMETRY
650	1	4	_aPROTEIN
650	1	4	_aPEPTIDE
650	1	4	_aPROTEOMICS
700	1	2	_aChamrád, I.
700	1	2	_aSimerský, R.
700	1	2	_aLenobel, R.
700	1	2	_aNovák, O.
856	4	0	_uhttps://drive.google.com/file/d/16Fz99j_6ZxA1cQS3lqOnEkq4e9Ou0fHk/view?usp=drive_link _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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