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  • 1
    Electronic Resource
    Electronic Resource
    A calcium(2+) ion-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzyme (1976)
    s.l. : American Chemical Society
    Biochemistry 15 (1976), S. 2159-2167 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00655a020
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  • 2
    Electronic Resource
    Electronic Resource
    CONTINUATION OF SYMPOSIUM: FUNDAMENTAL PROPERTIES OF MUSCLE PROTEINS IMPORTANT IN MEAT SCIENCE: ROLE OF NEW CYTOSKELETAL ELEMENTS IN MAINTENANCE OF MUSCLE INTEGRITY (1984)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 8 (1984), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Evidence suggests that desmin, titin and nebulin, three recently discovered proteins, have cytoskeletal roles in muscle cells. The three proteins have been purified from mature skeletal muscle and partially characterized. Properties of the three proteins are described, with special regard to their probable roles and importance in maintaining muscle cell integrity. Results will be shown that demonstrate ability of purified desmin to self-assemble into synthetic 10-nm (intermediate) diameter filaments. Taken together with immunoelectron microscope results (Richardson et al. 1981), it is evident that desmin is the major component of 10-nm filaments of mature skeletal muscle cells and that the desmin filaments link adjacent myofibrils at their Z-line levels and seemingly tie the myofibrils into the cell cyto-skeleton. Desmin is degraded at about the same rate as is the highly susceptible troponin-T in bovine semitendinosus muscle postmortem. Alterations in desmin and other recently discovered cytoskeletal proteins would be expected to disrupt muscle cell integrity and to have marked effects on properties of muscle important to its use as food.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1984.tb00310.x
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  • 3
    Electronic Resource
    Electronic Resource
    Effects of Salt and Pyrophosphate on the Physical and Chemical Properties of Beef Muscle (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 53 (1988), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effects of sodium chloride (NaCl) and pyrophosphate (PP) were examined by treating beef sternomandibularis muscle tissue and isolated beef myofibrils with various concentrations of NaCl, with and without 10 mM PP. Gel electrophoresis showed that higher NaCl concentrations (1.0M 〉 0.7M 〉 0.4M) increased the extraction of titin, myosin, and other myofibrillar proteins from beef tissue and that the inclusion of 10 mM PP to NaCl solutions enhanced the extraction of those proteins. Beef tissue water-holding capacity (WHC) was increased by higher NaCl concentrations and the presence of 10 mM PP. Increased myofibrillar/cytoskeletal protein extraction, especially titin, was associated with increased beef myofibril swelling and increased beef muscle WHC.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1988.tb09252.x
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  • 4
    Electronic Resource
    Electronic Resource
    MECHANISM OF CALCIUM TRANSPORT IN SARCOPLASMIC RETICULUM (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 264 (1975), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1975.tb31494.x
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  • 5
    Electronic Resource
    Electronic Resource
    MYOFIBRIL FRAGMENTATION AND SHEAR RESISTANCE OF THREE BOVINE MUSCLES DURING POSTMORTEM STORAGE (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 41 (1976), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Samples were removed from bovine longissimus (L), semitendinosus (ST) and psoas major (PM) muscles at 1, 2, 3, 6, 7, 10 or 13 days postmortem stored at 2°C or 25°C. Myofibril fragmentation index (MFI) and Warner-Bratzler (W-B) shear-force values were determined on steaks from each muscle. Myofibril fragmentation index (MFI) was determined quantitatively by measuring the absorbance of a myofibril suspension. It was observed that MFI increased during postmortem storage for L and ST, but increased only slightly for PM. These results paralleled those changes in myofibrils observed with phase and polarized light microscopy. Both MFI and W-B shear-force values changed greatly from 1 to 3 days postmortem with a lesser change occurring after 3 days in L and ST muscles. In PM muscle, however, only a slight change in MFI and W-B shear-force occurred during postmortem storage. Elevated storage temperature (25°C) caused an accelerated change in both MFI and W-B shear-force in L and ST muscles; however, storage temperature had little effect on PM muscle. L and ST muscles responded similarly to postmortem storage, but PM muscle was characteristically different from the L and ST muscles. These findings demonstrate the differences and similarities of muscles to postmortem storage and further elucidate the role of myofibrillar proteins in meat tenderness.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1976.tb14384.x
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  • 6
    Electronic Resource
    Electronic Resource
    A comparison of shortening and Z line degradation in post-mortem bovine, porcine, and rabbit muscleJournal Paper J-6254 of the Iowa Agriculture and Home Economics Experiment Station, Ames, Iowa, Project 1549. Supported in part by Public Health Servie Research grant GM 12488. (1970)
    New York, NY [u.a.] : Wiley-Blackwell
    American Journal of Anatomy 128 (1970), S. 117-135 
    Details
    ISSN: 0002-9106
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Ultrastructural changes in bovine, porcine, and rabbit muscle have been studied during the first 24 hours post-mortem. Samples were taken for phase and electron microscopy immediately after death, after 4, 8, and 24 hours of post-mortem storage at 2° and 37°C, and after 24 hours post-mortem at 16° and 25°C. The results show that two kinds of structural changes occur in muscle during the first 24 hours post-mortem: (a) a variable amount of shortening, this shortening occurring via a sliding of filaments in all species and at all post-mortem storage temperatures examined, and (b) degradation of the Z line, and at higher storage temperatures, of the M line also. Shortening of unrestrained muscle occurs soonest post-mortem at 37°C in all three species and is completed within four hours post-mortem in porcine and rabbit muscle and within eight hours post-mortem in bovine muscle. Post-mortem short-ening of unrestrained rabbit and porcine muscle is greatest at 37°C (sarcomere lengths of 1.5 μ); shortening of rabbit muscle is minimal at 2°C (sarcomere lenght of 1.7 μ), but shortening of porcine muscle is minimal at 25°C (sarcomere length of 1.8 μ) and is slightly greater at 2°C (sarcomere length of 1.6 μ) than at 16°C. Post-mortem shortening of bovine muscle is greatest at 2°C (sarcomere length of 1.3 μ), is minimal at 16-25°C (sarcomere length of 1.8 μ), and increases between 25-37°C (sarcomere length of 1.5 μ at 37°C). Sarcomere length measurements show that some variation occurs in the extent of post-mortem shortening within the same muscle.Z line degradation occurs sooner post-mortem and to a greater extent at storage temperatures of 25°C or above than at temperatures of 16°C or below. Also, bovine muscle Z lines are clearly more resistant to post-mortem degradation than porcine or rabbit muscle Z lines. Loss of fibrillar structure in porcine or rabbit muscle Z lines occurs during the first four hours post-mortem at 37°C, but eight hours of post-mortem storage at 37°C are required to cause loss of fibrillar structure of bovine muscle Z lines. After 24 hours at 25 or 37°C, Z lines of rabbit and porcine muscle are usually completely absent; M lines are also frequently absent in this muscle.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aja.1001280109
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