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  • 1990-1994  (5)
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  • 1
    Electronic Resource
    Electronic Resource
    Postmortem Changes in ATP, Creatine Phosphate, and Lactate in Sardine Muscle (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 56 (1991), 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: Postmortem changes were followed in sardines stored in ice. Fast (“white”) muscle creatine phosphate began decreasing from 25 μmol/ g immediately after death. ATP concentration remained about 10 μmol/ g and began decreasing after 2 hr when rigor mortis onset was observed. ATP decreased rapidly when creatine phosphate concentration reached a level similar to ATP, and was 2 μmol/g after 8 hr when full rigor was observed. Lactate accumulation proceeded parallel to ATP degradation (correlation coefficient r = -0.995) and the degree of rigor mortis (r = -0.989). In contrast, sardine slow muscle was low in creatine phosphate (1 μmol/g) and ATP (5 μmol/g), both of which decreased immediately after death. Lactate accumulation was low in this muscle and correlation with rigor mortis progress was lower (r = -0.902) than for fast muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1991.tb07998.x
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  • 2
    Electronic Resource
    Electronic Resource
    Acceleration of Physicochemical Change in Carp Muscle by Washing in Either Chilled or Heated Water (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 55 (1990), 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: “Arai” (washing) is a traditional cooking method of fish preparation in Japan. Carp muscle slices were washed in water (49°C for 15 sec, or 0°C for 10 min), and examined for physical and biochemical changes. At 49°C, rigor-mortis was accelerated, resulting in a marked decrease of muscle slice thickness. ATP degradation proceeded faster at 49°C than at 0°C. Arai treatment at 49°C increased myofibrillar Mg2+ - AT-Pase activity 8-9 times in the absence of Ca2+, but did not affect activity in the presence of Ca2+ as much, giving only a 1.2 times increase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1990.tb05204.x
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  • 3
    Electronic Resource
    Electronic Resource
    Thermal Degradation of Paralytic Shellfish Poison (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 56 (1991), 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: Components of paralytic shellfish poison (PSP) were heated under various conditions, and examined for changes in toxicity and in HPLC and TLC behaviors. The thermal degradation of PSP components progressed as a first order reaction, at different rates depending upon component and temperature. A mixture of gonyautoxin 2 and gonyautoxin 3 when dissolved in water and heated at 100°, 110°, and 120°C (180 min) retained 39, 17, and less than 3%, respectively, of initial toxicity. A mixture of gonyautoxin 1 and gonyautoxin 4 was more therrnolabile; i.e. it retained little toxicity when heated at 120°C for 60 min. HPLC and TLC analyses demonstrated that heating under those conditions converted PSP components into other substances.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1991.tb08643.x
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  • 4
    Electronic Resource
    Electronic Resource
    Short Thermal Treatment Effect on Carp Myofibril and Sarcoplasmic Reticulum: Possible Mechanisms in Rigor Mortis Acceleration by “Arai” Treatment (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 56 (1991), 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: Inorganic γ-phosphate liberation from adenosine 5′-triphosphate (ATP) by carp myofibrillar ATPase was measured at 0-60°C to elucidate mechanisms in rigor mortis acceleration of sliced carp muscle during washing at a moderately high temperature. ATP splitting within 20 sec in the presence of 5 mM MgCl2 plus 0.25 mM CaCl2 was maximal at 45°C, which agreed well with the commercially adopted condition for preparing carp “arai” muscle. In addition, the maximum Ca2+ uptake by sarcoplasmic reticulum was observed at 30°C and decreased at higher temperatures. The acceleration of carp muscle rigor mortis at around 45°C was suggested to be partly due to enhancement of myofibrillar Mg2+-ATPase activity by increase of intracellular Ca2+ concentration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1991.tb05349.x
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  • 5
    Electronic Resource
    Electronic Resource
    Changes of carp myosin subfragment-1 induced by temperature acclimation (1991)
    Springer
    Journal of comparative physiology 161 (1991), S. 141-146 
    Details
    ISSN: 1432-136X
    Keywords: Temperature ; Acclimation ; Carp ; Myosin ; Myosin subfragment-1 ; ATPase activity ; Thermostability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Heavy meromyosin subfragment-1 (S1) was prepared by α-chymotrypsin from myosin of carp acclimated to either 10°C or 30°C for a minimum of 5 weeks. The objective of these studies was to document thermally-induced changes in the myosin molecule and to extend previous observations. Ca2+- and K+ (EDTA)-ATPase activities of cold-acclimated carp S1 were 1.1 and 0.8 μmol Pi·min-1·mg-1, respectively, and these values did not differ significantly from those of warm-acclimated carp. The inactivation rate constant (KD) of S1 from cold-acclimated carp was 32.1x10-4· s-1, compared to 13.2x10-4·s-1 for warm-acclimated carp. The maximum initial velocity of acto-S1 Mg2+-ATPase activity at pH 7.0 in 0.05 M KCl was 9.3 s-1 with cold-acclimated carp, about 3.7 times higher than that for warm-acclimated carp. However, no significant difference was observed in the apparent affinity of S1 to actin. Peptides maps of the heavy chain of S1 were different and suggested distinct isoforms for the myosins from warm- and cold-acclimated muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00262876
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