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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 30 (1965), S. 0 
    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 activity of 17 or 18 specific enzymes in the longissimus dorsi muscle of five beef and 18 pork carcasses was followed by histochemical procedures. Beef samples were removed from carcasses within 10 min up to 20 days port-mortem, and pork samples within 16 min up to 24 and/or 48 hr post-mortem. The beef carcasses were submitted to so-called normal cooling procedures. However, one side of each of 13 pork carcasses was placed at –29°C, while the other side was subjected to 37°C for the first 41/2–5 hr post-mortem.In beef muscle, the histochemical activity of lactate dehydrogenase, alpha-glycerophosphate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase, TPN diaphorase, and DPN diaphorase showed a steady decrease with increasing time post-mortem. Reactions for both alcohol dehydrogenase and glutamate dehydrogenase were very weak or entirely absent at 48 hr post-mortem and all subsequent sampling periods. Positive reactions for glucose-6-phosphate dehydrogenase and beta-hydroxybutyrate dehydrogenase were observed in the initial samples only. No acid phosphatase, leucine amino peptidase, or 6-phosphogluconate dehydrogenase activity was detected in any of the samples.In pork muscle, the activity of lactate dehydrogenase, alpha-glycerophosphate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase, and DPN diaphorase was slightly weaker at both 0 and 24 hr post-mortem than similar activity in beef muscle. Alcohol dehydrogenase activity was weaker than that observed for the above enzymes, while the activity of glutamate dehydrogenase was of intermediate intensity. Traces of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activity were observed in only a portion of the initial samples. Similarly, weak reactions for beta-hydroxybutyrate dehydrogenase were observed only at 0 hr post-mortem. None or only weak activity was observed for malic dehydrogenase, and TPN diaphorase activity was unexplainably absent from all samples. Moderate levels of cytochrome oxidase activity were observed at both 0 and 24 hr post-mortem. LTDPG-glycogen transferase was completely inactivated by the 37°C treatment post-mortem, but the treatment had a less marked effect upon phosphorylase and branching enzyme. The presence of acid and alkaline phosphatase activity in muscles of 7 carcasses suggested that a degenerative condition existed in these muscles.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 4 (1957), S. 0 
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: SUMMARY. Objectives of the investigation were to: (1) ascertain whether, on the basis of enzyme inhibition, localization, and staining intensity, multiple phosphatases exist in Tetrahymena pyriformis W; (2) show activity values for phosphatase in specimens of T. pyriformis W from various ages and types of culture solutions; and (3) test the reliability of the Ca-cobalt technique for demonstration of phosphatase in cell nuclei.Complete inhibition of phosphatases (Ca-cobalt) was obtained with semi-carbazide, HCI and 0.2 m citrate buffer, pH 5.5. Potassium cyanide (0.01 m) tended to activate phosphatase with adenosinetriphosphate and inhibited phosphatase with Na-glycerophosphate, adenosine-5-phosphate, adenosine-3-phosphate, glucose-1-phosphate, and creatine phosphate solutions. A differential inhibition of phosphatase was obtained with inhibitors other than KCN.Phosphatase-active areas were in essentially the same intracellular position in all substrate solutions with the exception of enzyme-active areas in organisms from tryptone-MgCl2-citrate (0.01 m, pH 5.5) solutions; in the latter, both nuclear and cytoplasmic activity was evident. Organisms from tryptone-MgCl2-citratel (0.02 m), and vitamin-enriched tryptone solutions exhibited abundant cytoplasmic phosphatase with the azo-dye procedure. On the other hand, cytoplasmic phosphatase was not demonstrated with the Ca-cobalt procedure.Results obtained with enzyme inhibitors, various substrate solutions and evaluation of staining intensities suggest but do not demonstrate that 3 phosphomonoesterases, which hydrolyze glycero-phosphate, adenosine-5-phosphate, and adenosinetriphosphate, exist in Tetrahymena pyriformis W.Nuclear reactions obtained with the Ca-cobalt procedure were believed to be artifacts, with the exception of reactions obtained with cells from tryptone-MgCl2-citrate solutions subsequent to incubation in adenosinetriphosphate solution.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 36 (1971), S. 0 
    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
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Morphology 94 (1954), S. 587-615 
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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