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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Inflammation research 49 (2000), S. 60-61 
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 66 (2001), 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: Color analysis on apple and potato slices coated with calcium caseinate or whey protein solutions showed that the 2 coatings efficiently delayed browning by acting as oxygen barriers. The antioxidant properties of the films were realized using a model allowing the release of oxidative species by electrolysis of saline buffer. Whey proteins were a better antioxidant capacity than calcium caseinate. Furthermore, addition of carboxymethyl cellulose (CMC) to the formulations significantly improved their antioxidative power. Best scavenging of oxygen free radicals and reactive oxygen species was found for films based on whey proteins and CMC which inhibited by 75% the formation of colored compounds produced by the reaction of the oxidative species with N,N-diethyl-p-phenylenediamine.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract An inflexion point on the dependence of the swine kidney diamine oxidase activity upon the temperature was found at 40–43°C, suggesting a conformational transition. The activation energies with putrescine as substrate calculated from the Arrhenius plots were 38.23 kcal/mol for the temperature interval 25–40°C and only 15.14 kcal/mol for the range 45–60°C. These values suggest two different conformations, one corresponding to the interval below 40°C and another one between 43–60°C, with an intermediate transitory form corresponding to the inflexion point at 40–43°C. For various temperature decades within 10–60°C, peculiarQ 10 values in the range 1.37–3.00 (differing from the usual valueQ 10=2), were obtained. The non-strictly Arrhenius curves, the activation energies and the inflexion point were quite similar with and without 0.05% polyvinylalcohol. This particular temperature effect found for swine kidney diamine oxidase is similar to the one reported for bovine serum amine oxidase. An increased enzyme thermal stability was obtained in the presence of high molecular weight polyvinylalcohol.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1436-2449
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Summary Unlike usual polyhydroxilic packing materials for liquid chromatography based on cross-linked agarose, CL-amylose and CL-dextrans (Sephadex), the cross-linked PVA gels exhibit an increase of swelling properties with the reticulation degree, up to a certain limit. Afterwards more advanced reticulation degrees induce a decrease in swelling capacities just as in case of other cross-linked polyhydroxilic polymers. This abnormal behaviour of CL-PVA was supposed as being due to the interchain hydrogen associations. IR spectra, X-ray data and 8 M urea treatments strongly supported our supposition pointing out a maximum association by hydrogen bonds in CL-PVA gels with a reduced degree of reticulation.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1612-1112
    Keywords: Chromatographic material ; Ceruloplasmin ; Immobilization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary When mammalian plasma was passed through a chromatographic material containing aminoethyl functional groups, ceruloplasmin was selectively retained. At a specific ionic strength of the eluant buffer, a single chromatographic peak corresponding to the electrophoretically homogeneous purified ceruloplasmin was eluted. This single-step procedure is easy to perform and gave a purification yield of more than 60%. The direct immobilization of the ceruloplasmin, while it was still adsorbed and concentrated at the basal part of the gel bed (last stage of the purification), was achieved by carbodiimide treatment, with coupling yields of 50–70%. The immobilized ceruloplasmin retained about 100% of its enzymatic activity. Kinetic studies have shown a decreased affinity of the immobilized protein for the substrate and a maximal velocity of 81% as compared to the free protein. The immobilized ceruloplasmin was much more resistant to proteolytic attack than the free enzyme which is highly protease sensitive. Using pronase and thermolysine proteases, the activity of free ceruloplasmin was entirely lost in few hours. However, under similar conditions, the immobilized ceruloplasmin exhibited a high stability, maintaining its integral activity even after 24 hours of proteolytic attack.
    Type of Medium: Electronic Resource
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