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Literature summary for 1.11.2.2 extracted from

  • Shazeeb, M.; Xie, Y.; Gupta, S.; Bogdanov Jr., A.
    A novel paramagnetic substrate for detecting myeloperoxidase activity in vivo (2012), Mol. Imaging, 11, 433-443.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
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 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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