Abstract
Porphyrinogens with modified propionate side chains bearing methyl substituents were found to be modest substrates for coproporphyrinogen oxidase; the results indicate that alteration of the substituents involved in secondary binding interactions has a comparable affect to modifying the side chain that undergoes degradation at the catalytic site.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Binding Sites
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Catalysis
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Chickens
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Chromatography, High Pressure Liquid
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Coproporphyrinogen Oxidase / drug effects*
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Coproporphyrinogens / chemistry*
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Erythrocytes / drug effects
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Erythrocytes / enzymology
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In Vitro Techniques
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Kinetics
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Methylation
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Protein Binding
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Structure-Activity Relationship
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Substrate Specificity
Substances
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Coproporphyrinogens
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coproporphyrinogen III
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Coproporphyrinogen Oxidase