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Characterization and application of proline-selective proteases.
Portašiková, Jasmína Mária ; Man, Petr (advisor) ; Kádek, Alan (referee)
Peptide bond formed by proline is resistant to most known proteases, therefore the discovery and isolation of proteases cleaving after this amino acid opens up new possibilities not only for protein characterization but also for industrial, food or pharmaceutical aplications. Aspergillus niger prolyl endopeptidase (AnPEP) is a proline-selective protease that is commercially available in a variety of products. In this bachelor thesis cleavage preferences of proteases AnPEP (Clarity Ferm) and ProAlanase (Promega) were characterized and compared. The effect of different conditions on the specificity of proteases, while cleavaging the mixture of model proteins was examined within this work. AnPEP cleavage preferences were characterized on complex protein mixtures and its immobilized form was tested as well. [IN CZECH] Keywords: ProAlanase, AnPEP, H/D exchange, structural proteomics, imobilized proteases [IN CZECH]

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