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pro vyhledávání: '"Enda Miland"'
Publikováno v:
Analytical Chemistry. 69:1674-1681
Amperometric organic- and aqueous-phase peroxide biosensors were prepared with native and N-hydroxysuccinimide ester (NHS)-modified horseradish peroxidase (HRP). The e-amino functions of the free lysine residues of HRP were selectively modified with
Publikováno v:
Journal of Chemical Technology & Biotechnology. 67:227-236
Horseradish peroxidase (HRP) catalyses the oxidation of toxic aromatic compounds, especially phenols, in the presence of hydrogen peroxide. Reaction products polymerise to form insoluble precipitates which readily separate from aqueous solution, unli
Publikováno v:
Enzyme and Microbial Technology. 19:242-249
Horseradish peroxidase (HRP) has been chemically modified with the homobifunctional cross-linking reagents suberic acid n -hydroxysuccinimide ester (SA-NHS) and ethylene glycol bis-succinimidyl succinate (EG-NHS) yielding derivatives of native HRP wi
Publikováno v:
Enzyme and Microbial Technology. 19:63-67
Thermal stability of horseradish peroxidase (HRP) has been enhanced by acetylation with acetic acid n -hydroxysuccinimide ester (AA-NHS) under mild conditions. The half-life at 65°C was increased fivefold. This modification has also resulted in grea