Journal of Food Science · 1964 · 58 citations · 7 references
Life SciencesAnimal SciencesBiochemistryCellular MetabolismMetabolismProtein BiochemistryAmino Acid MetabolismDisulfide Bond FormationGlutathione MetabolismSulfur ChemistrySulfur CompoundsSulfur MetabolismCysteine ContributionsCysteine-related Sulfur CompoundsGlutathione PrecursorsHydrogen Sulfide MetabolismHydrogen Sulfide PrecursorsMethionine Sulfur CompoundsMethionine-derived Sulfur CompoundsMethionine-related Sulfur Compounds
SUMMARY About 90% of the hydrogen sulfide (H 2 S) produced by heated chicken muscle comes from muscle protein. To identify specific H 2 S precursors, the identity, quantity, and H 2 Sproducing capability of sulfur compounds in chicken muscle were investigated. The only sulfur compounds found in muscle nonprotein were methionine, taurine, and glutathione. Of these, only glutathione produced H 2 S. Therefore the principal H 2 S precursor in chicken muscle nonprotein is sulfur, occurring as eystine and/or cysteine in the tripeptide glutathione. Since the only sulfur compounds reported in chicken muscle protein are methionine, cystine, and/or cysteine, and since methionine does not produce H 2 S, the sulfur in the H 2 S produced by muscle protein must also come from cystine and/or cysteine. Glutathione gives off H 2 S about 180 times as fast as does chicken muscle protein, but, because there is approximately 1 to 2 thousand times as much protein as glutathione in muscle, protein is the principal H 2 S precursor. Since cystine plus cysteine, sulfur in protein and in glutathione is the only H 2 S precursor, the rate of H 2 S evolution from heated chicken muscle can be approximately predicted from its cystine content.
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THE FREE AMINO ACIDS OF HUMAN BLOOD PLASMA
William H. Stein, Stanford Moore · Journal of Biological Chemistry · 1954 · 937 citations · Full text
CHICKEN FLAVOR: THE SOURCE OF THE MEAT FLAVOR COMPONENT
R. J. Bouthilet · Journal of Food Science · 1951 · 38 citations