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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 86 (1964), S. 781-787 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 92 (1970), S. 6723-6728 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 3 (1964), S. 1596-1600 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Analytical chemistry 32 (1960), S. 960-966 
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
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  • 5
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Analytical chemistry 33 (1961), S. 22-22 
    ISSN: 1520-6882
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
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  • 6
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 54 (1932), S. 3469-3485 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Annales geophysicae 17 (1999), S. 1397-1410 
    ISSN: 0992-7689
    Keywords: Ionosphere (ionosphere irregularities) ; Magnetospheric physics (magnetosphere-ionosphere interactions) ; Radio science (ionospheric physics)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract Day-time Pc 3–4 (≃5–60 mHz) and night-time Pi 2 (≃5–20 mHz) ULF waves propagating down through the ionosphere can cause oscillations in the Doppler shift of HF radio transmissions that are correlated with the magnetic pulsations recorded on the ground. In order to examine properties of these correlated signals, we conducted a joint HF Doppler/magnetometer experiment for two six-month intervals at a location near L = 1.8. The magnetic pulsations were best correlated with ionospheric oscillations from near the F region peak. The Doppler oscillations were in phase at two different altitudes, and their amplitude increased in proportion to the radio sounding frequency. The same results were obtained for the O- and X-mode radio signals. A surprising finding was a constant phase difference between the pulsations in the ionosphere and on the ground for all frequencies below the local field line resonance frequency, independent of season or local time. These observations have been compared with theoretical predictions of the amplitude and phase of ionospheric Doppler oscillations driven by downgoing Alfvén mode waves. Our results agree with these predictions at or very near the field line resonance frequency but not at other frequencies. We conclude that the majority of the observations, which are for pulsations below the resonant frequency, are associated with downgoing fast mode waves, and models of the wave-ionosphere interaction need to be modified accordingly.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 18 (1982), S. 121-129 
    ISSN: 1432-1432
    Keywords: Varanus ; Lizard ; Claw ; Keratin ; Electrophoresis ; Protein ; Fractionation ; Glycine ; Tryptophan
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The outer shell of translucent keratin has been dissected from the claws of the lizard,Varanus gouldii. It is free of calcium and hydroxyproline, in contrast to the fibrous support, and contains proteins rich in glycine (28 residues %) and half-cystine (13%). These proteins have been obtained in soluble form by treatment with 2-mercaptoethanol in 8M urea at pH 11 followed by alkylation with iodoacetate to giveS-carboxymethyl kerateines. The three major components resolved by SDS polyacrylamide gel electrophoresis have been isolated by fractional precipitation with ammonium sulfate followed by chromatography on DEAE-cellulose or Sephadex. Two of the components, low in tryptophan content, appear to be homologous and are relatively homogeneous with respect to both size and charge whereas the third, a tryptophan-rich material, appears to contain about 20 different molecular species as judged by gel electrophoresis in urea at pH 8.9. The molecular weights of two of the isolated omponents (the tryptophan-rich and the major of the two tryptophanpoor components) are about 13000 as determined by equilibrium ultracentrifugation studies. The major lizard claw proteins are therefore similar in size and glycine content to the proteins of avian beak and claw but differ in containing more cystine and less tyrosine. On the other hand, the reptilian proteins resemble the mammalian high-tyrosine proteins (Type II) in cystine content and overall amino acid composition, but differ in size with the lizard proteins being larger. It is suggested however that they are unlikely to be homologous.
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 44 (1979), 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: Extracellular protease and lipase from Pseudomonas fragi significantly (P 〈 0.05) decreased color stability of sterile beef at 4°C and sterile beef extract at 4°C and 21°C. Concentrations of free fatty acids (FFA) in enzyme-treated sterile beef samples were significantly (P 〈 0.05) higher than in sterile controls held at 4°C indicating hydrolysis of glycerides by lipase from P. fragi. Concentrations of nonprotein nitrogen (NPN) and free amino acids in sterile beef extract treated with extracellular enzyme and held at 4°C and 21°C were significantly (P 〈 0.05) higher than in controls indicating proteolysis by protease from P. fragi. This was confirmed by SDS-polyacrylamide gel electrophoresis of enzyme-treated beef extract stored at 4°C for 6 days. Sephadex G-100 gel filtration and poly-acrylamide disc electrophoresis indicated that the molecular size and electrophoretic mobility of the protease and lipase were similar.
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 42 (1977), 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: Efficacies and optimum application conditions of three sanitizers (chlorine, 200–250 ppm; acetic acid, 4.0%; and quaternary ammonium, 3.78 g/liter) were determined. Variables were three rates of flow of sanitizer (1.7, 3.4 and 6.8 liters/min), washed and unwashed meat, warm (38°C) and cold meat (3.3°C), and two pressures of sanitizer application (3.5 and 14.0 kg/cm2). Results were averaged over other variables providing the following data for individual variables. Acetic acid gave a high initial average decrease in counts (−1.47 log), and counts decreased (−1.79 log) up to 48 hr after sanitization. Chlorinated solution caused an initial mean difference of −0.31 log and a difference after 48 hr of 0.53. The quaternary ammonium compound produced differences of −0.79 and −0.03 log in immediate and 48-hr counts. Acetic acid and hypochlorite were nonselective, but the quaternary sanitizer allowed more oxidase positive, nonfermentative bacteria to survive.
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