Combination of Protoporphyrin IX with Sperm Whale Apomyoglobin
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چکیده
منابع مشابه
Conformational changes in sperm-whale metmyoglobin due to combination with antibodies to apomyoglobin.
1. No ferrihaem was detected in the precipitate formed by metmyoglobin with an antiserum to apomyoglobin and the extinction at 410mmu of metmyoglobin, due to ferrihaem, was decreased by the univalent fragments of apomyoglobin antibodies. It was concluded that the combination of apomyoglobin antibodies with metmyoglobin caused the release of ferrihaem. As the removal of ferrihaem from metmyoglob...
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Considerable attention has been devoted recently to the study of conformational changes occurring during enzyme-substrate interaction (1, 2). Presumably the nature of the interaction between apoproteins and their prosthetic groups is essentially similar to that between enzymes and substrates, with the exception that no catalytic step occurs subsequent to the initial binding. Studies of the phys...
متن کاملL-histidine-containing peptides as models for the interaction of copper (II) and nickel (II) ions with sperm whale apomyoglobin.
1. The association and ionization constants for nickel (II) and a selection of L-histidine-containing peptides have been computed together with the constants for copper (II) and acetylglycylglycyl-L-histidylglycine. 2. A close parallel between the titration behavior of copper (II) apomyoglobin complexes and model peptides has been obtained on the assumption that 1 of the 4 bound metal ions is s...
متن کاملSimultaneous liquid-chromatographic determination of zinc protoporphyrin IX, protoporphyrin IX, and coproporphyrin in whole blood.
We describe a method for simultaneously measuring concentrations of coproporphyrin, zinc protoporphyrin IX, and protoporphyrin IX in whole blood by liquid chromatography, with use of reversed-phase ion-pair system, fluorometric detection, and internal standardization. Each analysis requires 10 microL of whole blood and 15 min total analysis time. Analytical recovery ranged from 84 to 92%, day-t...
متن کاملProperties of protoporphyrin-apomyoglobin complexes and related compounds.
The conformation of the 1: 1 complex of protoporphyrin IX and apomyoglobin was studied by circular dichroism, potentiometric titration, and reaction with bromoacetate. Circular dichroism studies indicate that protoporphyrin and heme similarly affect the o-helix content of apomyoglobin. The apparent number of normal imidazoles in the protoporphyrin-apomyoglobin complex, as judged by reactivity t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1965
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)97458-2