Title : Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins.

Pub. Date : 1993 Jun

PMID : 8390491






4 Functional Relationships(s)
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1 Protein-bound tyrosyl residues exposed to myeloperoxidase, H2O2, and L-tyrosine were oxidized to o,o"-dityrosine, a stable product of the tyrosyl radical. dityrosine myeloperoxidase Homo sapiens
2 The requirement for free L-tyrosine and H2O2 for dityrosine formation and the inhibition by heme poisons support the hypothesis that myeloperoxidase catalyzes the cross-linking of proteins by a peroxidative mechanism involving tyrosyl radical. dityrosine myeloperoxidase Homo sapiens
3 We speculate that protein dityrosine cross-linking by myeloperoxidase may play a role in bacterial killing or injuring normal tissue. dityrosine myeloperoxidase Homo sapiens
4 The intense fluorescence and stability of biphenolic compounds may allow dityrosine to act as a marker for proteins oxidatively damaged by myeloperoxidase in phagocyte-rich inflammatory lesions. dityrosine myeloperoxidase Homo sapiens