Abstract
Hemerythrin is proposed as an alternative to hemoglobin-based blood substitutes. In contrast to hemoglobin, hemerythrin exhibits negligible reactivity towards oxidative and nitrosative stress agents (peroxide, nitric oxide, nitrite). Protocols for attachment of polyethylene glycol and glutaraldehyde cross-linking of Hr are described. These derivatizations appear to have favorable effects on O(2) affinity and autoxidation rates for use in blood substitutes. Based on lessons learned from hemoglobin-based blood substitutes, these derivatizations should also help limit extravasation and antigenicity of a hemerythrin-based blood substitute.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Blood Substitutes / chemistry*
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Glutaral / chemistry
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Hemerythrin / chemistry*
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Hemerythrin / genetics
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Hemerythrin / metabolism
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Hemoglobins / chemistry
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Hemoglobins / metabolism
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Hydrogen Peroxide / metabolism
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Models, Molecular
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Nematoda / genetics
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Nitric Oxide / metabolism
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Oxidation-Reduction
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Oxygen / metabolism
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Polyethylene Glycols / chemistry
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Spectrophotometry, Ultraviolet
Substances
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Blood Substitutes
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Hemerythrin
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Hemoglobins
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Recombinant Proteins
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Nitric Oxide
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Polyethylene Glycols
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Hydrogen Peroxide
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Oxygen
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Glutaral