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“…These values remained constant for 72 hours, the maximum aging period used in their studies. Chajuss and Spencer (1962b) also proposed a mechanism for postrigor tenderization which was compatible with their belief that rigor was at least partially due to oxidation of muscle sulfhydryl groups to disulfidewhich would link protein molecules. They postulated that postrigor tenderization was due to sulfhydryl-disulfide exchange reactions, which could produce randomization and relaxation of the network formed at the onset of rigor.…”
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“…These values remained constant for 72 hours, the maximum aging period used in their studies. Chajuss and Spencer (1962b) also proposed a mechanism for postrigor tenderization which was compatible with their belief that rigor was at least partially due to oxidation of muscle sulfhydryl groups to disulfidewhich would link protein molecules. They postulated that postrigor tenderization was due to sulfhydryl-disulfide exchange reactions, which could produce randomization and relaxation of the network formed at the onset of rigor.…”
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“…They demonstrated that the post-mortem disappearance of-SH groups paralleled the onset of rigor (Chajuss and Spencer, 1962b). The -SH content of muscle which had been aged in air decreased from an initial concentration of 9.9 X 1CM to about 6.5 X 10-6 mole per gram after entering the rigor state.…”
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“…Thus muscle that is tender initially, becomes tough, then becomes tender, The possibility that these postmortem changes in tenderness are related to the sulfhy-dryl-disulfide composition of muscle is attractive. Chajuss et al (1962) proposed that conversion of protein sulfhydryl groups to disulfide bonds may confer stained configurations on muscle proteins and stabilize the rigor state. In support of this proposal they reported observations of decreases in thiol concentration in excised chicken muscle aged in air at 2527°C; nitroferricyanide was used to measure sulfhydryl content.…”
Section: Introduction Chemicalmentioning