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001-es BibID:	BIBFORM050956
Első szerző:	Monzo, Alex
Cím:	Proteolytic enzyme-immobilization techniques for MS-based protein analysis / Alex Monzo, Edit Sperling, András Guttman
Dátum:	2009
ISSN:	0165-9936
Megjegyzések:	Protein digestion utilizing proteases (e.g., trypsin, Lys C and other proteolytic enzymes) is one of the key sample-preparation steps in contemporary proteomics, followed by liquid chromatography coupled to mass spectrometry (MS). Tryptic digestion is traditionally performed in aqueous solutions, usually applying the enzyme and the sample in a 50:1 protein-to-protease ratio. Long digestion times (up to 24 h), auto-digestion sub-products and poor enzyme-to-substrate ratio are common issues with liquid-phase protein-digestion processes. The use of enzymes immobilized onto solid supports can minimize these problems by increasing enzyme-to-substrate ratios, significantly speeding up digestion times and reducing autolysis. The other main goal of protease immobilization is to obtain rugged, efficient enzyme reactors.In this article, we review the most important proteolytic enzyme-immobilization techniques with the main emphasis on fabrication of trypsin microreactors and nanoreactors and their utilization in bottom-up proteomics. We also discuss data reportedly obtained using the various immobilization protocols with respect to enzyme activity and MS-sequence coverage.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Enzyme immobilization Mass spectrometry Protease Protein analysis Protein digestion Proteolytic enzyme Proteomics Trypsin microreactor Trypsin nanoreactor Tryptic digestion
Megjelenés:	Trac-Trends in Analytical Chemistry. - 28 : 7 (2009), p. 854-864. -
További szerzők:	Sperling Edit Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	TéT A-10/2006 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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