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  • 1
    Electronic Resource
    Electronic Resource
    TEXTURAL DETERIORATION OF RED HAKE AND HADDOCK MUSCLE IN FROZEN STORAGE AS RELATED TO CHEMICAL PARAMETERS AND CHANGES IN THE MYOFIBRILLAR PROTEINS (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 44 (1979), 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 present study involved the measurement of fish muscle texture by both objective and subjective means. Reliable methods for the evaluation of fish texture as well as interpretation of results are discussed. The study demonstrated that significant correlations between the methods could be achieved if carefully controlled conditions were maintained. The presence of dimethylamine in frozen hake (Urophycis chuss) appeared to be a good chemical indicator of toughness whereas the extractable protein nitrogen was not as reliable. Data suggest that although the enzymatic formation of formaldehyde was a major factor in the toughening of red hake, other factors probably contribute to the textural deterioration observed during cold storage. It is evident that haddock (Melunogrammus aeglefinus) toughens when stored at relatively high temperatures (-5°C) and like hake, experiences a loss of water-holding capacity although no formaldehyde accumulates in the tissues. The molecular basis of toughening in fish was examined by SDS gel electrophoresis. Apparently, the formaldehyde produced by the TMAO-ase enzyme system in red hake resulted in the covalent cross linking of troponin and myosin light chains, forming higher molecular weight aggregates. Changes at the molecular level were not detected by this method in haddock. Textural changes in this species are not as pronounced as those of hake and are most likely due to secondary bonds such as hydrogen or electrostatic.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1979.tb08470.x
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  • 2
    Electronic Resource
    Electronic Resource
    Stereoselectivity for the (R)-Enantiomer of HA-966 (l-Hydroxy-3-Aminopyrrolidone-2) at the Glycine Site of the N-Methyl-d-Aspartate Receptor Complex (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 55 (1990), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: HA-966 (1-hydroxy-3-aminopyrrolidone-2) is an antagonist at the glycine allosteric site of the N-methyl-d-aspartate receptor ionophore complex. Unlike presently known glycine antagonists, HA-966 is chiral. We report stereoselectivity for the (R)-enantiomer at the glycine antagonist site. In [3H]glycine binding, the (R)-enantiomer has an IC50 of 4.1 ± 0.6 μM. The racemic mixture has an IC50 of 11.2 ± 0.5 μM, whereas (S)-HA-966 has an IC50 greater than 900 μM. In glycine-stimulated [3H]l-[1-(2-thienyl)cyclohexyl] piperidine binding, the (R)-enantiomer inhibits with an IC50 of 121 ± 61μM, whereas the racemic mixture has an IC50 of 216 ± 113 μM and (S)-HA-966 is inactive. The inhibition by (R)-HA-966 can be prevented by the addition of glycine. (R)-HA-966 and racemic HA-966, but not (S) HA-966, also prevent N-methyl-d-aspartate cytotoxicity in cortical cultures. The (R)-enantiomer and, less potently, the (S)-enantiomer inhibit N-methyl-d-aspartate-evoked [3H]norepinephrine release from rat hippocampal slices (IC50 values of about 0.3 mM and 1.6 mM, respectively), but only the inhibition by (R)-HA-966 is reversed by added glycine. In glutamate-evoked contractions of the guinea pig ileum, (R)-HA-966 causes a glycine-reversible inhibition (IC50 of about 150 μM), whereas (S)-HA-966 is much less potent (IC50 of greater than 1mM). These results demonstrate stereoselectivity of the glycine antagonist site of the N-methyl-d-aspartate receptor complex in a variety of tissues and assays. The stereoselectivity also confirms the specificity of N-methyl-d-aspartate receptors in glutamate-evoked contractions of the guinea pig ileum, and supports their similarity to central N-methyl-d-aspartate receptors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1990.tb03145.x
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  • 3
    Electronic Resource
    Electronic Resource
    Down-Regulation in Peripheral α2-Receptor Function by the Administration of Imipramine and the Coadministration of Imipramine and Yohimbine (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 463 (1986), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1986.tb21576.x
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  • 4
    Electronic Resource
    Electronic Resource
    STABILITY OF LEAN AND FATTY FISH FILLETS IN HYPOBARIC STORAGE (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 45 (1980), 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: Fillets of lean (cod) and fatty fish (herring and mackerel) were stored in a hypobaric chamber at −1.1, −0.55, and 0°C under a pressure of 10 mm Hg. The atmosphere was changed twice hourly, and had a relative humidity greater than 95%. The growth of bacteria in the filets was slowed, and a qualitative shift in the micro-flora occurred, compared with fillets held at 0°C on ice. The rate of development of rancidity in the fatty fillets was also decreased. Because of these changes, a 10-15% extension in keeping times of hypobarically stored fillets was observed at 0°C. The storage life of fillets at low pressure was further extended by the decrease of storage temperature and by treating the fillets with Na, H EDTA. EDTA did not increase the storage life of the fatty fillets.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1980.tb07545.x
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  • 5
    Electronic Resource
    Electronic Resource
    ω-Grammotoxin blocks action-potential-induced Ca2+ influx and whole-cell Ca2+ current in rat dorsal-root ganglion neurons (1994)
    Springer
    Pflügers Archiv 426 (1994), S. 214-220 
    Details
    ISSN: 1432-2013
    Keywords: ω-Grammotoxin ; ω-Conotoxin ; Dihydropyridines ; Ca2+ channel ; Ca2+ current ; Dorsal-root ganglion neurons
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Field-potential stimulation of rat dorsal-root ganglion (DRG) neurons evoked action-potential-mediated transient increases in intracellular free calcium concentration ([Ca2+]i) as measured by indo-1-based microfluorimetry. Field-potential-evoked [Ca2+]i transients were abolished by tetrodotoxin, and their dependence on stimulus intensity exhibited an abrupt threshold. ω-Conotoxin GVIA (ω-CgTx, 100 nM) inhibited action-potential-mediated Ca2+ influx by 79%, while nitrendipine (1 μM) had little effect. ω-Grammotoxin SIA (ω-GsTx, 267 nM), a peptide toxin purified from the venom of the tarantula spider, Grammostola spatulata, blocked action-potential-mediated Ca2+ influx as effectively as did ω-CgTx, suggesting that ω-GsTx blocks N-type Ca2+ channels. In contrast to block by ω-CgTx, the block produced by ω-GsTx reversed upon washout of the peptide. ω-GsTx (270 nM) blocked 80%, and ω-CgTx (1 μM) blocked 64%, of whole-cell Ca2+ current (I Ca) elicited by step depolarization to 0 mV from a holding potential of −80 mV. ω-GsTx completely occluded inhibition of I Ca by ω-CgTx. However, when applied after ω-CgTx, ω-GsTx produced an additional inhibition of 27%, indicating that ω-GsTx also blocked a non-N-type Ca2+ channel. BayK8644 (1 μM) elicited an increase in I Ca in the presence of maximally effective concentrations of ω-GsTx, suggesting that ω-GsTx does not block L-type channels. Thus, ω-GsTx displays a selectivity for Ca2+ channel subtypes which should prove useful for studying Ca2+ channels and Ca2+-channel-mediated processes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00374774
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