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Lability and reactivity of nonheme protein bound nitrite



Lability and reactivity of nonheme protein bound nitrite



Journal of Food Science 48(4): 1204-1207



Nitrite treated nonheme protein was separated from the free nitrite of the reaction mixture by Sephadex G-15 column chromatography. Spectral analysis (absorbance at 330 nm) indicated that tryptophyl residues of the protein was modified with the NO group. The protein-nitrite complex was not stable, decomposing faster at lower pH and higher temperatures. As the extent of the decomposition increased with time, an increasing amount of nitrite was detected by the Association of Official Analytical Chemists method, indicating that the Griess reagent reacted with nitrite after it was regenerated from the NO group. When myoglobin was incubated with the nitrosated protein, nitrosyl hemochrome could be extracted from the reaction mixture in the presence of ascorbic acid. The results indicate the potential reversibility of the protein-nitrite reaction. [This study relates to meat processing.].

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Accession: 005787220

Download citation: RISBibTeXText

DOI: 10.1111/j.1365-2621.1983.tb09192.x


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