Recombinant immobilized rhizopuspepsin as a new tool for protein digestion in hydrogen/deuterium exchange mass spectrometry

0330788 - MBÚ 2010 RIV GB eng J - Článek v odborném periodiku
Rey, M. - Man, Petr - Brandolin, G. - Forest, E. - Pelosi, L.
Recombinant immobilized rhizopuspepsin as a new tool for protein digestion in hydrogen/deuterium exchange mass spectrometry.
Rapid Communications in Mass Spectrometry. Roč. 23, č. 21 (2009), s. 3431-3438. ISSN 0951-4198. E-ISSN 1097-0231
Výzkumný záměr: CEZ:AV0Z50200510
Klíčová slova: mass spectrometry * recombinant immobilized rhizopuspepsin * protease
Kód oboru RIV: CE - Biochemie
Impakt faktor: 2.695, rok: 2009

This paper reports on expression, ioslation and testing of protease type XVIII from Rhizopus sp. Recombinant protease proved to be much more efficient than the commercially availabe crude extract. Moreover it showed excellent cleavage specifity and efficiency when immobilized to the POROS resin. The use of this protease enhance spatial resolution achievable in hydrogen/deuterium exchange coupled to mass spectrometry
Trvalý link: http://hdl.handle.net/11104/0005489