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1.11.2.2
analysis
detection of myeloperoxidase activity in vivo by use of a paramagneitc substrate. The sensing probe is obtained by replacing the reducing substrate serotonin with 5-hydroxytryptophan. The resulting probe bis-hydroxytryptophan-gadolinium diethylenetriamine pentaacetic acid in vitro improves solubility in water, acts as a substrate, induces cross linking of proteins in the presence of myeloperoxidase,produces oxidation products which bind to plasma proteins and does not follow first order reaction kinetics. Bis-hydroxytryptophan-gadolinium diethylenetriamine pentaacetic acid is retained for up to five days in myeloperoxidase-containing sites and cleared faster than serotonin diethylenetriamine pentaacetic acid from enzyme-negative sites
725986
1.11.2.2
medicine
loading macrophages with exogenous myeloperoxidase could enhance their microbicidal activity, potentially useful therapeutic application
661675
1.11.2.2
medicine
the enzyme is an interesting target for anti-inflammatory therapy
671909
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