2005
DOI: 10.1016/j.jmmm.2005.02.030
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Magnetic enzyme reactors for isolation and study of heterogeneous glycoproteins

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Cited by 24 publications
(14 citation statements)
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“…The reaction conditions for protein fragmentation by trypsin reactors were optimized (Table 3), following an approach similar to this described by Korecká et al [51,52]. Briefly, the type of buffer, ions, pH, temperature, E:S ratio, digestion time, surfactant, and K M , as well as the composition of the storage solution were varied.…”
Section: Characterization Of Proteolytic Microreactorsmentioning
confidence: 99%
“…The reaction conditions for protein fragmentation by trypsin reactors were optimized (Table 3), following an approach similar to this described by Korecká et al [51,52]. Briefly, the type of buffer, ions, pH, temperature, E:S ratio, digestion time, surfactant, and K M , as well as the composition of the storage solution were varied.…”
Section: Characterization Of Proteolytic Microreactorsmentioning
confidence: 99%
“…Magnetic particles provide a universal system with additional convenience, consistency, stability, ease of handling and exceptional flexibility compared to standard chromatography resinos. Hydrophilic macroporous bead cellulose is carrier with a high surface area, with easily modified OHÀ groups for covalent ligand attachment, minimal nonspecific binding for common protein and peptide molecules, no tendency to aggregate and excellent flow characteristics [13]. Such characteristics of carrier combined with improved immobilization strategy could significantly improve the conditions for enzyme catalysis of azo dyes degradation and other industrial applications.…”
mentioning
confidence: 99%
“…Various enzymes including glucoamylase (Bahar & Celebi, 1999), cytochrome C oxidase (Cuyper & Joniau, 1992), β-lactamase (Gao et al, 2003), chymotrypsin (Izmaĭlov et al, 2000, Rebelo et al, 2010, alcohol dehydrogenase , glucose oxidase, galactose oxidase, urease (Varlan & Sansen Ann Van, 1996), neuramidinase (Bilkova et al, 2002), papain (Korecká et al, 2005), Dnase (Rittich et al, 2002), Rnase (Horák et al, 2001), etc. can be immobilized via chemical bonds on coated or embedded magnetic particles.…”
Section: Property Improvement Of the Immobilized Enzymes On Magnementioning
confidence: 99%