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  • 1980-1984  (3)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 181 (1980), S. 1227-1235 
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: A pair of polymers may interact with each other through hydrogen bond and form a polymer complex. Such polymer complex formation is affected by several chemical and physical factors, especially by solvent properties. This solvent effect was studied in the complex formation of poly(methacrylic acid) with a series of proton-accepting polymers in aprotic solvents. The extraordinary behaviour of polymer complexes in dimethyl sulfoxide was well explained in terms of the strong interaction between proton-donating polymer and dimethyl sulfoxide. In addition, a stronger proton-accepting polymer, viz. poly(N,N-dimethyl-N′,N′,N″,N″-tetramethylenephosphoramide), was synthesized. This polymer could form a polymer complex with poly(methacrylic acid) through hydrogen bond even in dimethyl sulfoxide. Selective polymer complex formation was achieved by controlling such solvent properties.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 182 (1981), S. 1407-1414 
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: The interactions of human serum proteins with synthetic macromolecules were studied in heterogeneous solution systems. An alternating copolymer of styrene with maleic anhydride was crosslinked by diamines with different number of methylene groups varying from 2 to 10, and the degree of crosslinking (mole fraction of amide linked units) was changed from 7 to 43% in order to elucidate the effects of pore size, density of ionic site, and flexibility of the macromolecules. The adsorption of serum proteins on the resins was studied with human serum albumin and γ-globulin as typical proteins in human serum. The resins were dispersed in phosphate buffer solutions, and these were mixed with the phosphate buffer solutions of albumin and/or γ-globulin. After a suitable period of incubation at 20°C, the mixed solutions were centrifuged. The degree of protein-adsorption was determined from the remaining amounts of proteins in the supernatant as measured by U.V. spectrometry. It was observed that the adsorption of albumin was influenced by the subtle balance of hydrophobicity and hydrophilicity of the resin. On the other hand, γ-globulin was adsorbed not only by the hydrophobic resin but also by the hydrophilic (ionic) resin. The resin which was crosslinked to 16% by hexamethylenediamine showed high affinity towards γ-globulin at pH 7,4. Selective adsorption was also possible: Almost all of the γ-globulin and only little of the albumin were adsorbed within half an hour at 20°C by the use of this resin.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Publication Date: 1980-01-01
    Print ISSN: 0040-4039
    Electronic ISSN: 1873-3581
    Topics: Chemistry and Pharmacology
    Published by Elsevier
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