HAVLIŠ, Jan, Tatiana ŠTOSOVÁ, Marek ŠEBELA and René LENOBL. Proteolytické enzymy: význam pro proteomiku (Proteolytic enzymes: Significance for proteomics). Chemické listy. Praha: Czech Chemical Society, 2005, vol. 99, No 12, p. 896-905. ISSN 0009-2770.
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Basic information
Original name Proteolytické enzymy: význam pro proteomiku
Name in Czech Proteolytické enzymy: význam pro proteomiku
Name (in English) Proteolytic enzymes: Significance for proteomics
Authors HAVLIŠ, Jan, Tatiana ŠTOSOVÁ, Marek ŠEBELA and René LENOBL.
Edition Chemické listy, Praha, Czech Chemical Society, 2005, 0009-2770.
Other information
Original language Czech
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher Czech Republic
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 0.445
Organization unit Faculty of Science
UT WoS 000234182000005
Keywords in English TANDEM MASS-SPECTROMETRY; AMINO-ACID SEQUENCE; PROTEIN IDENTIFICATION; POLYACRYLAMIDE-GELS; QUADRUPOLE-TIME; LYSOBACTER-ENZYMOGENES; CHEMICAL-MODIFICATION; CARBOXYPEPTIDASE-Y; PSEUDOMONAS-FRAGI; MEMBRANE-PROTEINS
Tags AMINO-ACID SEQUENCE, CARBOXYPEPTIDASE-Y, CHEMICAL-MODIFICATION, LYSOBACTER-ENZYMOGENES, MEMBRANE-PROTEINS, POLYACRYLAMIDE-GELS, PROTEIN IDENTIFICATION, PSEUDOMONAS-FRAGI, QUADRUPOLE-TIME, TANDEM MASS-SPECTROMETRY
Tags Reviewed
Changed by Changed by: doc. Mgr. Jan Havliš, Dr., učo 743. Changed: 2/7/2009 18:59.
Abstract
Proteolytic enzymes (peptidases) are important tools for proteomic research. This article reviews their application to digestion of proteins, which commonly precedes the mass spectrometry analysis of proteins. In the opening part, mechanism of proteolysis is described together with a detailed introduction to classification and nomenclature of enzymes. The following part brings an overview of proteolytic enzymes that are currently used in expression and functional proteomics including their properties and specificity. The review continues with reports on assays of proteolytic activity and computer prediction of peptide cleavage. The methodology of in-solution and in-gel digestion of samples and the use of peptidases for cleavage of proteins on membrane surfaces is also mentioned. Furthermore, chemical modifications of peptidases for improving their stability to autolysis and thermal inactivation are documented. Peptidase treatment of hydrophobic proteins in solutions containing organic solvents are also mentioned. Finally, new perspectives of proteolysis in shotgun proteomics are outlined.
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