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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 15 (1967), S. 1112-1117 
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 916-922 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The crystal structures of three metal complexes of troponin C (TnC) have been determined and refined where the two occupied structural Ca2+ sites in the C domain have been substituted by Mn2+, Cd2+ and Tb3+. The X-ray intensity data were collected to 2.1, 1.8 and 1.8 Å resolution, respectively, on the three metal complexes, which are isomorphous with Ca-TnC. The three complexes have r.m.s. deviations of 0.27, 0.25 and 0.35 Å, respectively, for all protein atoms, from Ca-TnC. Irrespective of the charge on the metal (+2 or +3), the occupied sites 3 and 4 exhibit a distorted pentagonal bipyramidal coordination, like Ca-TnC, with seven ligands, six from the 12-residue binding loop and the seventh from a water molecule. Mn2+ at site 4 seems to display a longer distance to one of the carboxyl bidentate ligands representing an intermediate coordination simulating the six-coordinate Mg2+. The carboxyl O atoms of the bidentate Glu12 are displaced on the side of the equatorial plane passing through the remaining three ligands with one O atom closer to the plane (Δ of 0.11 to 0.76 Å) than the other (Δ of 0.93 to 1.38 Å). The two axial ligands are an aspartic carboxyl O atom and a water molecule. The metal is displaced (0.18 to 0.56 Å) towards the water facing the water channel.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 43 (1978), 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 reaction of sodium nitrite with tryptophan was studied spectrophotometrically; the N-nitroso reaction product had an absorption peak at 330 nm and the absorption maximum of tryptophan was shifted from 277 nm to 266 nm. In model systems, where sodium nitrite was 10 mM and tryptophan was 1.0 mM, the reaction proceeded rapidly at pH 4.0 and very slowly at pH 5.5 or higher. Experiments with acetyltryptophan and dipeptides showed that if the primary amino group of tryptophan was blocked, then nitrosation of the indole nitrogen was promoted. Tryptophan was formed when the N-nitroso reaction product was subjected to gel filtration in the absence of nitrite. If the concentration of reactants and pH are compared for model systems favorable for formation of nitrosotryptophan and for cured meats, it is apparent that the environment for nitrosation of tryptophan is unfavorable in most cured meats.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 39 (1974), 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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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 40 (1975), 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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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 37 (1972), 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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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 32 (1967), 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: SUMMARY— Techniques are described for the electron microscopic evaluation of a meat emulsion. Fat globules as small as 0.1 μ in diameter were observed to have distinct protein membranes. The continuous phase of the emulsion was fibrous, but homogeneous. After thermal processing the globule membranes were highly disrupted and the protein of the continuous phase was coagulated into dense, irregular zones.
    Type of Medium: Electronic Resource
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  • 8
    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
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  • 9
    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 from homogenates of normal and pale, soft, exudative (PSE) porcine muscle at 0 and 24 hr post-mortem and examined by electron microscopy. No differences were observed between normal and PSE myofibrils obtained at death. PSE myofibrils prepared at 24 hr post-mortem had more granular appearing filaments and wider Z lines than normal myofibrils at 24 hr. The PSE heavy sarcoplasmic reticulum fraction obtained at death had a higher proportion of granular material than the same fraction from normal muscle. Several structural differences between the other PSE and normal fractions were also observed, especially at 24 hr postmortem. This study indicated that the composition of the subcellular fractions changed with time post-mortem and that this change should be considered when analyzing biochemical data from these fractions. However, the differences observed could not explain the large changes in calcium accumulating ability that have been shown to occur post-mortem.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 48 (1983), 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: Nitrite treated nonheme protein was separated from the free nitrite of the reaction mixture by Sephadex G-15 column chromatography. Spectral analysis (absorbance at 330 nm) indicated that tryptophyl residues of the protein had been modified with the NO group. The protein-nitrite complex was not stable, decomposing faster at lower pH and higher temperature. As the extent of the decomposition increased with time, an increasing amount of nitrite was detected by the AOAC method, indicating that the Griess reagent reacted with nitrite after it was regenerated from the NO group. When myoglobin was incubated with the nitrosated protein, nitrosyl hemochrome could be extracted from the reaction mixture in the presence of ascorbic acid. The results indicate the potential reversibility of the protein-nitrite reaction.
    Type of Medium: Electronic Resource
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