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Targeting Heme with Single Domain Antibodies
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| 7.13 MB | Adobe PDF |
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Heme, i.e. iron (Fe) protoporphyrin IX, functions as a prosthetic group in a variety of
hemoproteins that participate in vital biologic functions essential to sustain life.
Heme is a highly reactive molecule, participating in redox reactions, and
presumably for this reason it must be sequestered within the heme pockets of
hemoproteins, controlling its reactivity. However, under biological stress conditions,
hemoproteins can release their prosthetic groups, generating “free heme”, which
binds loosely to proteins or to other molecules and presumably acquires unfettered
redox activity. Moreover, a growing body of evidence supports the notion that “free
heme” can act in a vasoactive, pro-inflammatory and cytotoxic manner when
released from a subset of these hemoproteins, such as extracellular hemoglobin,
generated during hemolytic conditions. (...)
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Biochemistry