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  • Blackwell Publishing Ltd  (29)
  • 1
    Electronic Resource
    Electronic Resource
    The Effect of pH-Temperature Treatments on the Calcium Accumulating Ability of Purified Sarcoplasmic Reticulum (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: Pig sarcoplasmic reticulum fragments obtained from the longissimus dorsi muscle at 0- and 24-hours post-mortem were purified by salt extraction and density gradient centrifugation. The calcium uptake activity of 0-hour purified preparations was more than 20-fold higher than that from 24-hr old muscles, but there was no significant difference between fractions for calcium activated ATPase activities. When observed electron microscopically after negative staining, the ultrastructures of the 0. and 24-hour membrane fragments were found to be essentially identical. Incubation of isolated sacroplasmic reticulum fragments at pH 7.2 and 37°C or pH 5.6 and 0°C caused negligible inhibitoin of their calcium accumulating ability. However, treatment at pH 5.6 and 37°C for 1 hr almost completely abolished the sarcoplasmic reticulum calcium uptake. Thus it appears that low muscle pH and high temperature may be responsible for the inactivation of the calcium accumulating ability of the sarcoplasmic reticulum that occurs in situ.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1969.tb12109.x
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  • 2
    Electronic Resource
    Electronic Resource
    Post-Mortem Changes in Subcellular Fractions from Normal and Pale, Soft, Exudative Porcine Muscle. 1. Calcium Accumulation and Adenosine Triphosphatase Activities (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– Myofibrillar, mitochondrial, heavy sarcoplasmic reticulum and light sarcoplasmic reticulum fractions were isolated by differential centrifugation of homogenates from normal and pale, soft, exudative (PSE) porcine muscle at various times post-mortem. Calcium uptake was measured using a solution containing45Ca++. The oxalate-stimulated calcium accumulating ability of the subcellular fractions declined 5-10 fold between 0 and 24 hr post-mortem. The major portion of this decline occurred in the first hour after death in fractions from PSE muscle but was more gradual in the normal fractions. The ATPase activities of normal and PSE fractions obtained at death did not differ significantly. These activities increased with time post-mortem in most normal fractions but decreased in those from PSE muscle. The subcellular site of ATP hydrolysis post-mortem was discussed. The results obtained point to the potential importance of the relaxing, factor in muscle post-mortem.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1969.tb00901.x
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  • 3
    Electronic Resource
    Electronic Resource
    Prediction of the Time Course of Rigor Mortis Through Response of Muscle Tissue to Electrical Stimulation (1966)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 31 (1966), 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: A technique based on muscle response to electrical stimulation was shown to be useful in predicting, within 10 min of exsanguination, the time course of rigor mortis, rate of postmortem glycolysis, and ultimate color-morphology rating. The response of an excised muscle to electrical stimulation was highly associated with post-mortem muscle properties. The excitability threshold (lowest voltage at which contraction resulted) was found to be high in muscles which had a short time course of rigor mortis, fast postmortem glycolysis, and pale, soft, and exudative (PSE) ultimate gross morphology; and low in muscles with a long time course of rigor mortis, slow post-mortem glycolysis, and ultimately normal color-morphology. Strength of contraction (at 5, 10, 25, and 50 volts) was observed to be highest in muscles which exhibited long rigor, slow glycolytic rate, and normal color-morphology. The duration of contractility (maintained under repeated stimulation at 2 cycles/see) was also noted to be longer in this type of muscle. Multiple-regression analysis indicated that up to 87% of the variability in color-morphology rating could be predicted by combining the various parameters of muscle response to electrical stimulation. Breed differences were observed which must be taken into account when using prediction equations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1966.tb15408.x
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  • 4
    Electronic Resource
    Electronic Resource
    Red and White Fiber Content and Associated Post-Mortem Properties of Seven Porcine Muscles (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: The red fiber content of several porcine muscles was estimated by a histochemical method (affinity for Sudan Black B due to high intracellular lipid content) and a biochemical method (high succinic dehydrogenase activity). Even though the muscles varied widely in total lipid content, the histochemical method was comparable to the biochemical method in categorizing porcine muscles as red or white. Red muscles (〉 40% red fibers) contained greater myoglobin concentrations and generally had longer post-rigor sarcomeres than white (〈 30% red fibers) muscles. Interrelationships of percent red fibers, succinic dehydrogenase activity, fat content, glycolytic rate, and post-rigor contraction state were discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1965.tb01872.x
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  • 5
    Electronic Resource
    Electronic Resource
    Prevention of Pale, Soft, Exudative Porcine Muscle Through Regulation of Ante-Mortem Environmental Temperature (1964)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 29 (1964), 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: Thirty-seven Poland China pigs of uniform weight were subjected to various (warm, cold, warm-cold) ante-mortem treatments. The warm treatment (42–45°C) resulted in rapid post-mortem glycolysis, rapid onset of rigor mortis at a low pH and high temperature, and the development of extremely pale, soft, and exudative musculature with a marked loss in juice retention and protein solubility. Although muscle characteristics improved markedly from cold treatment (1–3°C), the most desirable muscles were produced by the warm treatment followed immediately by cold treatment. The latter treatment resulted in lower muscle temperature and reduced levels of glycogen and certain glycolytic components at the time of death. These muscles exhibited a limited glycolysis, rapid onset of rigor mortis but at a low temperature and high pH, and appeared dark, dry, and firm, with superior juice retention and greater protein solubility. The cold-to-warm treatment failed to provide uniformity in the development of post-mortem changes in color and structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1964.tb01720.x
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  • 6
    Electronic Resource
    Electronic Resource
    Electron Microscopy of Post-Mortem Changes in Porcine Muscle (1963)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 28 (1963), 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: Electron microscopy was used to follow changes in porcine muscle during the 24-hr post-mortem chilling period. Ante-mortem subjection to elevated temperatures or to elevated temperatures and then chilling was used to produce different rates and magnitudes of change in post-mortem muscle color, texture, and water binding. Normal muscle exhibited a gradual disruption of sarcoplasmic components, with little if any change in the myofibrils. Muscle that went into rigor rapidly at a low pH and high temperature ultimately appeared soft, pale, and watery, and electron micrographs revealed a rapid disruption of sarcoplasmic components and some disorganization of the myo-filaments. Muscle that went into rigor rapidly at a high pH and a reduced temperature ultimately appeared dark, firm, and dry, and electron micrographs revealed a high degree of organization and preservation of myofibrillar structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1963.tb01674.x
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  • 7
    Electronic Resource
    Electronic Resource
    Functional analysis of the fsoC gene product of the F71 (fso) fimbrial gene cluster (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 4 (1990), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Contrary to what would be expected from data in the literature, mutations in the fsoC gene of the F71 (fso) P-fimbrial gene cluster do not completely block fimbrial biogenesis. fsoC mutants still express small amounts of fimbriae of normal length, which carry the non-adhesive minor subunit protein, FsoE, but lack the adhesin, FsoG. The FsoC protein operates at the same stage in fimbrial biogenesis as the FsoF and FsoG proteins. The data suggest that FsoC, FsoF and FsoG interact to form an initiation complex for fimbrial biogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1990.tb02018.x
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  • 8
    Electronic Resource
    Electronic Resource
    Immunocytochemical analysis of P-fimbrial structure: localization of minor subunits and the influence of the minor subunit FsoE on the biogenesis of the adhesin (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 4 (1990), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Antibodies recognizing the non-adhesive minor P-fimbrial subunrt protein E and the P-fimbrial adhesin were used in an immunocytochemical analysis of P-fimbrial structure. It was demonstrated that P-fimbriae of the serotypes F71, F72 and F11 carry their adhesin in a complex with protein E. These complexes are commonly found at the tip of the fimbrial structure. In P-fimbriae of serotype F9, expressed by the uropathogenic Escherichia coli strain 21086, adhesin-protein E complexes are localized at the tips as well as along the shafts of the fimbriae. Protein E of F71 fimbriae (FsoE) plays a catalysing role in the biogenesis of the adhesin, but has no effect on the eventual localization of the adhesin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1990.tb00694.x
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  • 9
    Electronic Resource
    Electronic Resource
    Biogenesis of F71 and F72 fimbriae of uropathogenic Escherichia coli: influence of the FsoF and FstFG proteins and localization of the Fso/FstE protein (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 2 (1988), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The F71 and F71 P-fimbriae of Escherichia coli are encoded by the fso (F seven one) and fst (F seven two) gene clusters, respectively (Van Die et al., 1984; 1985).With the immunocytochemical gold-labelling technique it was demonstrated that both the FsoE and FstE proteins are non-adhesive minor fimbrial sub-units located at the tip of the fimbrial structure. The FsoF and FstFG proteins play an important role in the initiation of polymerization of the minor and major subunits into the fimbrial structure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1988.tb00008.x
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  • 10
    Electronic Resource
    Electronic Resource
    Multifunctional nature of P fimbriae of uropathogenic Escherichia coli: mutations in fsoE and feoF influence fimbrial binding to renal tubuli and immobilized fibronectin (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 5 (1991), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: P fimbriae of the F71 serotype of Escherichia coli are composed of a major subunit, FsoA, and of three minor proteins named FsoG, FsoE, and FsoF. FsoG is the Galα(1–4)Gal-specific lectin. We assessed mutated recombinant strains each deficient in one fimbrial component for adhesion to frozen sections of rat cortical kidney and to fibronectin immobilized on glass. Rat kidney lacks the Galα(1–4)Gal-containing glycolipids. The fsoG mutant strain was as adhesive to sections of rat kidney and to fibronectin-coated glass as was the recombinant strain expressing the complete fso gene cluster. The fsoA mutant strain was highly adhesive to fibronectin and to kidney sections. In the rat kidney, the adhesion of these strains was predominantly localized to sites of basolateral membranes of tubuli. The fsoE and the fsoF mutant strains were slightly less adhesive to kidney structures and failed to adhere to fibronectin. The fsoE, fsoF double mutant strain adhered neither to fibronectin nor to kidney sections. None of the fso recombinant strains reacted with soluble fibronectin, suggesting that the interaction is dependent on the conformation of the fibronectin molecules. Recombinant strains expressing the F72, F8, F11, F13, and F14 serovariants of the P fimbria also showed adherence to immobilized fibronectin. The results show that in addition to binding to globoseries of glycolipids via the G protein, the P fimbriae of uropathogenic E. coli exhibit a tissue-binding property influenced by fsoE and fsoF gene products and with affinity for basolateral membranes and fibronectin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1991.tb01856.x
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