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  • 1
    Electronic Resource
    Electronic Resource
    Molecular Properties of Post-Mortem Muscle. 6. Effect of Temperature on Protein Solubility of Rabbit and Bovine Muscle (1969)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 34 (1969), 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– Studies were conducted to investigate the effect of temperature on the actin-myosin interaction of rabbit and bovine muscle during rigor and post-rigor shortening. Muscle was stored at four different temperatures (2°, 16°, 25° and 37°), corresponding to three types of post-mortem muscle shortening: cold, minimal and high temperature. These three types of shortening are presumably related to different states of the actin-myosin interaction in post-mortem muscle. Post-mortem tenderization may be the result of either actin-myosin dissociation or F-actin depolymerization.To detect the occurrence of either of these possible changes, two salt solutions, differing widely in their myofibrillar protein extracting abilities, were used to compare post-mortem myofibrillar protein solubility after different times of post-mortem storage and to provide information about the actin-myosin complex. Myofibrillar protein solubility of both rabbit and beef muscle in 0.5M KCl, 0.1M phosphate, pH 7.4, increased markedly with increasing post-mortem storage at temperatures up to 25deg;. Similar solubility changes were obtained with 1.1M Kl, 0.1M K phosphate, pH 7.4, but these changes were much smaller in magnitude. Solubility in both salt solutions, in general, decreased for muscle stored at 37°.Although time and temperature of post-mortem storage caused appreciable alterations in protein solubility, these alterations could not be directly related to changes in tenderness or sarcomere length or to species differences in the effects of temperature on post-mortem shortening. Viscosity, analytical ultracentrifugation, and ATPase assays all indicated the absence of “normal” actomyosin in all myofibrillar protein extracts in this study. It was suggested that the 1.1 M KI extracts contained G-actomyosin, but the available evidence indicated the presence of only myosin in 3-hr, 0.5 M KCI extracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1969.tb00915.x
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular Properties of Post-Mortem Muscle. 7. Changes in Nonprotein Nitrogen and Free Amino Acids of Bovine Muscle (1969)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 34 (1969), 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– Proteolysis and its relationship to tenderness were studied by measuring nonprotein nitrogen (NPN), free amino groups, and shear resistance during post-mortem aging of bovine muscle. Both NPN and free amino groups increased during post-mortem aging, indicating some degradation of proteins and/or peptides. However, neither the increase in NPN nor free amino groups was related to post-mortem tenderization since these quantities increased only after most of the improvement in tenderness had occurred. Much of the increase in NPN or free amino groups may originate from degradation of sarcoplasmic proteins or peptides. It is suggested that weakening or breaks at crucial points in the sarcomere, such as at the junction of the Z-line with the thin filaments, occur within the first 48-72 hr post-mortem and that this weakening or cleavage is responsible for tenderization. Cathepsin D may be responsible for this weakening but most of the available evidence is against proteolysis as the primary cause of post-mortem tenderization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1969.tb00918.x
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  • 3
    Electronic Resource
    Electronic Resource
    EFFECT OF POSTMORTEM STORAGE AND CALCIUM ACTIVATED FACTOR ON THE MYOFIBRILLAR PROTEINS OF BOVINE SKELETAL MUSCLE (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 42 (1977), 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: Myofibrils isolated from bovine longissimus (L), semitendinosus (ST) and psoas major (PM) muscles at-death and at 1, 2, 3, 6 and 10 days postmortem storage (2 and 25°C) were analyzed with sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. One of the subunits of troponin, troponin T, disappeared from L and ST muscle during postmortem storage at 25°C, and concurrently a 30,000 dalton component appeared. Storage of muscles at 25°C accelerated these changes in myofibrils from L and ST muscles, but SDS polyacrylamide gels of PM muscle changed little during storage at either 2 or 25°C. Crude preparations of a Ca2+-activated factor (CAF) were isolated from bovine L, ST and PM muscles. Total CAF activity was high and similar in L and ST muscles, but PM muscle contained less than half the total CAF activity of L and ST muscles. Incubation of purified CAF with myofibrils isolated from at-death muscle caused Z-disk degradation and disappearance of troponin T and the simulataneous appearance of a 30,000 dalton component. That incubation of purified CAF with purified troponin caused degradation of troponin-T to a 30,000-dalton component indicates that the 30,000-dalton component in whole myotibrils originates from troponin-T. The effects of CAF on Z-disk and troponin-T degradation and the relative total activity of CAF in L, ST and PM muscles are similar to the effects of postmortem storage in myofibril fragmentation, myotibrillar protein degradation and WB shear force values. These parallel effects indicate that the limited and. specific proteolysis of myofibrillar proteins is caused by a Ca2+-activated factor endogenous to the muscle cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1977.tb01233.x
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  • 4
    Electronic Resource
    Electronic Resource
    Molecular Properties of Post-Mortem Muscle. (1967)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 32 (1967), 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— Post-mortem changes in nucleoside triphosphatase activity of bovine myosin B have been studied by using several different modifiers with either 5 mM ATP or 5 mM ITP as substrate at ionic strengths (r/2) of 0.09, 0.19, or 0.52. Enzymic activity was determined by measuring the release of inorganic phosphate. There was very little difference in enzymic activity between myosin B isolated from prerigor, rigor (24 hr post-mortem) or post-rigor (312 hr post-mortem) muscle stored at either 2° or 16°C except that the specific activity of myosin B prepared from muscle stored for 12–24, hr post-mortem was higher than activity of myosin B prepared immediately after death. This increase cannot be explained in terms of rigor shortening, but suggests that a change in myosin conformation or in the nature of the actin-myosin interaction occurs in post-mortem muscle. If an actin-myosin interaction occurs during rigor mortis and if this association remains unchanged during extraction of myosin B, then the very low Mg++-modified myosin B enzymic activities obtained at Γ/2 = 0.19 and 0.52 indicate that this interaction is not irreversible. Extraction in the absence of ATP produced a myosin B whose ATPase activity was markedly inhibited by trace amounts of Mg++. This may be due to the absence of a-actinin in these myosin B preparations. No consistent differences in activation energies were found either at Γ/2 = 0.19 or 0.52 among the NTPase reactions of myosin B samples prepared from muscle after various times of post-mortem storage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1967.tb00828.x
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  • 5
    Electronic Resource
    Electronic Resource
    Effects of Germination on Proteins, Raffinose Oligosaccharides, and Antinutritional Factors in the Great Northern Beans (Phaseolus vulgaris L.) (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 48 (1983), 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: During 5 day germination, the major reserve proteins of the Great Northern bean (Phaseolus vulgaris L.) were substantially hydrolyzed. In vitro trypsin digestion of the extracted proteins up to 4 hr at 37°C indicated that the major storage proteins in germinated and the ungerminated seeds, although substantially hydrolyzed, could not be completely degraded. In vitro susceptibility of the extracted proteins was improved on moist heat treatment (97°C, 30 min). A substantial increase in soluble essential amino acids occurred during germination. Highest decrease in stachyose + raffimose (76.40%) was observed at the end of the third day of germination. Trypsin, chymotrypsin, and α-amylase inhibitory activities and phytic acid were reduced respectively by 62.9, 73.4, 67.1, and 57.8% after 5 days of germination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1983.tb05087.x
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  • 6
    Electronic Resource
    Electronic Resource
    Isometric Tension Changes and Shortening in Muscle Strips During Post-mortem Aging (1967)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 32 (1967), 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: Post-mortem tension changes of rabbit psoas and beef geniohyoideus and semitendinosus muscle were studied. A special device was constructed and used to measure these changes while holding the muscle isometrically. It has been possible to demonstrate a pattern of tension development and cessation in rabbit muscle at 24°C and in beef muscle at 0°, 10°, and 24°C. With rabbit muscle no tension development was detected at 0° or 10°C. Initiation of tension development is affected by the ante-mortem state of the animal as well as by temperature. The post-mortem tension decline occurs after the disappearence of ATP and evidently is not related to ATP degradation. Possible relationships between post-mortem tension changes and meat tenderness are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1967.tb01283.x
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