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  • 1
    Electronic Resource
    Electronic Resource
    Further Studies on Bovine Muscle Tenderness as Influenced by Carcass Position, Sarcomere Length, and Fiber Diameter (1965)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 30 (1965), 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: Interrelationships of fiber diameter, sarcomere length, and tenderness were studied in 12 bovine muscles of horizontally placed and vertically suspended carcass sides. In comparison with the horizontally placed sides, the vertically suspended sides had greater sarcomere lengths in the psoas major, latissimus dorsi, and rectus femoris muscles. Conversely, vertical suspension permitted the longissimus dorsi, gluteus medius, adductor, biceps femoris, and semitendinosus muscles to shorten in sarcomere length. In general the differences in sareomere lengths of muscles (between sides) were associated (r=–.82 P 〈.01) with differences in fiber diameter. Differences in fiber diameter (between sides) were highly related to differences in shear force (r= .73, P 〈.01, as were differences in sarcomere length (T = -.80, P 〈.01). When museles shortened, there were corresponding decreases in sarcomere length, increases in fiber diameter, and decreases in tenderness.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1965.tb01885.x
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  • 2
    Electronic Resource
    Electronic Resource
    Studies on Natural Actomyosin: Survey of Experimental Conditions (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: —Natural actomyosin was prepared from the longissimus dorsi of both bovine and rabbit. Rabbit actomyosin had about two times the ATPase activity of bovine muscle actomyosin. However, both types of natural actomyosin behaved in a similar manner with respect to ionic conditions. They were activated by Mg++ at low KCI (20–50 mM), inhibited by Mg++ at high KCI (100 mM) and activated by Ca++ at high KCI (100 mM). Bovine actomyosin, in contrast to rabbit actomyosin, did not show activation at low Mg++ (0.01 mM) in the alkaline pH range. Maleate, when used as Tris-Maleate buffer, inhibited superprecipitation of natural actomyosin from rabbit and bovine muscle. It was hypothesized that the low ATPase activity and the non-activation at low Mg++ in the alkaline pH range of bovine compared to rabbit actomyosin was a species difference.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1969.tb10351.x
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  • 3
    Electronic Resource
    Electronic Resource
    Studies on Bovine Natural Actomyosin 2. Physico-Chemical Properties and Tenderness of 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 made of physicochemical characteristics of natural actomyosin from bovine longissimus of different post-mortem ages and tenderness classifications. Reduced viscosity, ATP sensitivity, and “actin” content (polyethylene sulfonate treatment) were higher for natural actomyosin prepared from muscle 12-24 hr post-mortem than from pre-rigor muscle, which confirms previous reports for rabbit natural actomyosin. A higher actin to myosin ratio in actomyosin from muscle 12-24 hr was therefore postulated. A stronger interaction of actin and myosin in actomyosin from muscle 12-24 hr post-mortem than from pre-rigor or aged muscle was also suggested by reduced viscosity and ultracentrifugation data. Reduced viscosity differences between actomyosins from tough and tender muscle suggested a higher gel character in actomyosin from tough muscle. This possibly indicated a higher content of α-actinin. No consistent differences in ATP sensitivity, myosin and actin content of natural actomyosin of tough and tender muscle were found. Natural actomyosin from muscle aged post-mortem showed the appearance during analytical ultracentrifugation of an additional component which sedimented at about 11S to 12S. This component appeared in the actomyosin prepared from tender muscle after 24 hr but did not appear until 10 days in the actomyosin from tough muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1969.tb12092.x
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  • 4
    Electronic Resource
    Electronic Resource
    Tenderness and Associated Characteristics of Stretched and Contracted Bovine Muscles (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: The effects of muscle contraction state, carcass maturity, and post-mortem aging (4°C) on tenderness were studied on excised semitendinosus muscles of six A- and six E-maturity bovine carcasses. Fiber diameter was shown to be curvilinearly related with sarcomere length (R = .95 and .87 for A- and E-maturity groups, respectively). As muscles were shortened they had a larger percent area of fibers and a smaller percent area of both edomysial and perimysial material. Muscles of the A-maturity group were more tender (P 〈 .01) than those of the E-maturity group. Post-mortem aging resulted in tenderization in both A- and E-maturity groups at all states of contraction f-48 to +48% of the preexcised length); however, tenderness of contracted muscles did not reach acceptable levels even in 240 hr of aging. Tenderness was shown to be linearly related to fiber diameter (R = .82 and .87 for A- and E-maturity groups, respectively); however, the relationship with sarcomere length was curvilinear (R = .90 and .75 for A and E maturities, respectively). Post-mortem contraction of muscles was very effective in causing decreased tenderness, whereas the magnitude of tenderness increase was smaller than normal when muscles were stretched.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1967.tb01321_32_3.x
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  • 5
    Electronic Resource
    Electronic Resource
    Studies on Bovine Natural Actomyosin 1. Relationship of ATPase and Contractility to Tenderness of 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: The effects of muscle tenderness classification and of aging muscle postmortem on ATPase activity and superprecipitation of natural actomyosin were studied. Actomyosin from muscle 12- and 24-hr postmortem had higher ATPase activity than that from 0-hr, 5-day aged or 10-day aged muscle. However, ATPase activity did not usually return to the 0-hr level. No consistent differences were found in actomyosin ATPase activity after the various periods of aging for actomyosins from tough and tender muscle. Superprecipitation of actomyosin was used as a measure of contractility. Actmyosin from 12- and 24-hr postmortem muscle superprecipitated faster than that from 0-hr muscle. However, actomyosin from 5 and 10-day aged muscle superprecipitated less rapidly than that from 12- and 24-hr postmortem muscle. Superprecipitation was more rapid in actomyosin from tough muscle than tender muscle at low KCI concentrations, but this was not true at high KCI concentrations. This observation suggested that actomyosin from tough muscle had a stronger interaction or higher amounts of some protein factor such as α-actinin than did tender muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1969.tb12785.x
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  • 6
    Electronic Resource
    Electronic Resource
    Factors Affecting Collagen Solubility in Bovine Muscles (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— Solubility of intramuscular collagen was studied as affected by chronological maturity in 15 bovine longissimus dorsi and 15 semimembranosus muscles and as affected by post-mortem contraction state in the semitendinosus of 7 animals. Collagen solubility decreased significantly with each advancing maturity group in both longissimus dorsi and semimembranosus muscles. Collagen solubility was also higher (P 〈 0.05) in the longissimus dorsi than in the semimembranosus, except in the E maturity group. It was also related to panel tenderness in both muscles (r = 0.77 and 0.81 (P 〈 0.01) for longissimus dorsi and semimembranosus muscles, respectively. However, within-maturity group correlations of solubility of collagen and tenderness were low and nonsignificent.Collagen content did not differ significantly in longissimus dorsi muscles of animals of A, B, and E maturity groups; however, the semimembranosus had more collagen (P 〈 0.05) in E than in A and B maturity groups. Collagen content was not related (P 〉 0.05) to panel tenderness in either muscle (r =−0.42 and −0.48 for longissimus dorsi and semimembranosus, respectively). Neither collagen solubility nor collagen content was significantly affected by post-mortem contraction state. Furthermore, collagen solubility did not increase significantly with post-mortem aging up to ten days.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1967.tb00826.x
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