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  • 1975-1979  (2)
  • 1970-1974  (4)
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  • 1
    Electronic Resource
    Electronic Resource
    A Ca2+ion-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle (1976)
    s.l. : American Chemical Society
    Biochemistry 15 (1976), S. 2150-2158 
    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/bi00655a019
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    Paper (German National Licenses)
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  • 2
    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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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    MOLECULAR PROPERTIES OF POSTMORTEM MUSCLE. (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 37 (1972), 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
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1972.tb05838.x
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  • 4
    Electronic Resource
    Electronic Resource
    MOLECULAR PROPERTIES OF POSTMORTEM MUSCLE. 8. Effect of Postmortem Storage on α-Actinin and the Tropomyosin-Troponin Complex (1970)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 35 (1970), 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: SUMMARY– Effects of postmortem storage of rabbit muscle at 25° on the properties of α-actinin and tropomyosin-troponin-containing fractions prepared from this muscle were studied. Postmortem storage did not affect the amount of α-actinin or tropomyosin-troponin that could be extracted from rabbit myofibrils by water washes or by a 3-day, pH 8.5, low-ionic strength extraction. Myosin B prepared from postmortem muscle underwent turbidity development much faster than myosin B prepared from muscle immediately after death. This increased rate of turbidity development was probably not due to postmortem changes in α-actinin, since the ability of α-actinin to accelerate the ATPase (for abbreviations used in this paper, see list under References) activity or the turbidity response of reconstituted actomyosin suspensions gradually decreased, rather than increased, during postmortem storage. However, even after 14 days postmortem at 25°α-actinin retained some activity in both the ATPase and turbidity tests. Moreover, the increased rate of turbidity development of postmortem myosin B was probably not due to degradation of the tropomyosin-troponin complex, since postmortem storage affected the activity of this complex only slightly and, even after 14 days post-mortem, the tropomyosin-troponin complex still conferred some Ca++-sensitivity on reconstituted actomyosin suspensions. Myosin B prepared from postmortem muscle did not contain more active α-actinin than myosin B prepared from muscle immediately after death, but the F-actin-tropomyosin-troponin interaction was gradually weakened during postmortem storage without any evident degradation of F-actin and the tropomyosin-troponin complex themselves. The weakened F-actin-tropomyosin-troponin interaction probably caused loss of Ca++-sensitivity in myosin B prepared from postmortem muscle. Results of this study indicate that postmortem changes in α-actinin and the tropomyosin-troponin complex per se are not the primary cause of postmortem modification in the actin-myosin interaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1970.tb01976.x
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  • 5
    Electronic Resource
    Electronic Resource
    MOLECULAR PROPERTIES OF POST-MORTEM MUSCLE. 9. Effect of Temperature and pH on Tropomyosin-Troponin and Purified α-Actinin from Rabbit Muscle (1970)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 35 (1970), 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: SUMMARY– A study was done on the effects of in vitro storage of purified α-actinin, troponin, tropomyosin, and the tropomyosin-troponin complex on the activity of these protein fractions in the ATPase and superprecipitation assays. Storage was done at various combinations of temperatures between 0 and 40°C and pH values between 5.7 and 7.0. Even after 40 hr of storage, activities of purified tropomyosin and the tropomyosin-troponin complex were not affected by any combination of temperature and pH included in this study, but activities of purified α-actinin and troponin were almost completely lost after 16 hr at 40°C and pH 5.7. Storage for 40 hr at low pH (5.7) and low temperatures (0°C) did not affect the activity of either α-actinin or troponin, but 40 hr of storage at high temperatures (40°C) and neutral pH caused some loss in activity for both these proteins. This loss of activity caused by 40°C, pH 7.0 storage was much more noticeable in the case of troponin than in the case of α-actinin. Storage periods of 40 hr or longer were required before any loss of α-actinin activity could be detected at pH 7.0 and 40°C. Since most meat animal carcasses are chilled soon after exsanguination and attain muscle temperatures of 25°C or lower before the pH falls below 6.2, it is probable that α-actinin and tropomyosin-troponin activity remain almost unchanged in meat handled through normal market channels. However, myofibrillar tissue in those porcine animals whose musculature undergoes a very rapid post-mortem decline in pH so that values of 5.7 or less are reached while muscle temperatures are still 37°C or higher may lose much of its α-actinin and tropomyosin-troponin activity during the first 24 hr post-mortem.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1970.tb01977.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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