Ultrastructural and molecular changes in striated muscle during post-mortem shortening

Stromer, Marvin H.

doi:10.31274/rtd-180813-1477

Cited by 1 publication

(1 citation statement)

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“…An increase in meat tenderness, which occurs during cold storage after rigor mortis, results from the degradation processes in intra‐ and extracellular structures of muscle fibers (Palka 2000). Several review papers have summarized the postmortem changes in aged meat (Stromer et al. 1974; Bandman 1992).…”

Section: Introductionmentioning

confidence: 99%

Postmortem Changes in Myofibrillar Proteins of Goat Skeletal Muscles

Nagaraj

Santhanam

2005

Journal of Food Biochemistry

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Postmortem changes at 5C in myofibrillar proteins of longissimus dorsi (LD), biceps femoris (BF), semimembranosus (SM) and semitendinosus (ST) muscles and myofibrillar structure of LD muscle of goat were investigated. Muscle samples were immediately collected after killing, and from carcasses stored at 5C for 3, 6, 9, 12 and 20 days. The sodium dodecyl sulfate‐polyacrylamide gel electrophoresis of myofibrils indicated the appearance of a 30 kDa component, depending on the type of the muscles. A new 55 kDa component appeared in BF and SM muscles during postmortem. Titin I and nebulin also disappeared during storage. The disappearance of titin 1 and nebulin and the appearance of a 30 kDa component were confirmed by Western blot analysis. The Transmission Electron Microscopy studies showed that after 3 days postmortem, Z‐disks stayed unaltered. After 6 days postmortem, a little ultrastructural alteration was observed, and at 12 days postmortem a considerable degradation of Z‐disk ultrastructure was shown. The Z‐disk degradation, which results in the fragmentation of myofibrils and the appearance of 30 kDa components, is the major change observed in goat skeletal muscles during postmortem.

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Section: Introductionmentioning

confidence: 99%