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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 57 (1992), 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: Bovine SH-k-casein (k-C-pool) was fractionated into five components based on carbohydrate and sialic acid contents (k-C-P1 〈 k-C-P2 〈 k-C-P3 〈 k-C-P4 〈 k-C-P5) by ion-exchange chromatography (DEAE-cellulose). Chymosin susceptibility observed by monitoring changes in optical density during enzyme action, varied among the components. This was a reflection of the difference in self-association of the proteins in aqueous dispersion as determined by hydrophobic interaction chromatograph. There was an inverse relationship between surface hydrophobicity of the protein polymers (k-C-P2 〉k-C-P3 〉k-C-P4 〉 k-C-P5 〉 k-C-P4 〉 k-C-pool) and their susceptibility to chymosin at 37°C, pH 6.8 (k-C-pool 〉k-C-P1 〉k-C-P5 〉 k-C-P4 〉 k-C-P3 〉 k-C-P2). Mild heating decreased susceptibility and affected flocculation of all except the highly glycosilated components k-C-P4 and k-C-P5 reflecting amphipathicity imparted thermostability.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0894-3230
    Keywords: Organic Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Octaethyltetrathiaporphyrin dication, OTP2+, is electrochemically reduced by two successive electron-transfer processes to OPT0. OPT2+ forms intermolecular complexes with a series of π-donors. The association constants of the resulting complexes are controlled by the oxidation potentials of the π-donors and solvent properties. OTP2+ was incorporated into a Nafion membrane cast on a Pt electrode. Formation of OTP2+-π-donor complexes in the polymer membrane was followed by electrochemical and spectroscopic means. The association constants of the OTP2+-π-donor complexes in the Nafion membrane exhibit lower values than a homogeneous phase owing to the high ionic strength in the polyelectrolyte.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0894-3230
    Keywords: Organic Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The octaethyltetrathiaporphyrin dication, OTP2+, forms 1:1 intermolecular donor-acceptor complexes with NiII-, VIVO- and FeIII-octaethylporphyrins. The association constants of the complexes are governed by the oxidation potential of the metallo-octaethylporphyrins and by secondary electrostatic interactions. Octaethylporphyrin, H2OEP, forms intermolecular complexes with OTP2+. Kinetic analyses of the formation of the various complexes revealed the formation of a primary complex exhibiting the stoichiometry (OTP2+)2(H2OEP). This intermolecular complex transforms into a thermodynamically stabilized intermolecular assembly with a stoichiometry corresponding to (OTP2+)4H2OEP. The activation barrier associated with the conversion of the primary complex to the thermodynamically stabilized assembly is Ea = 16·5 kcal mol-1 (1 kcal = 4·184 kJ). The association constant of the complex (OTP2+)2(H2OEP) is K1 = 1·3 × 1010 M-2 and the equilibrium constant between the two coexisting intermolecular complexes (OTP2+)4(H2OEP) and (OTP2+)2(H2OEP) is K2 = 7·4.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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