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  • casein structure  (1)
  • sodium lauryl sulfate  (1)
  • 1
    ISSN: 1573-4943
    Keywords: Calcium binding ; casein structure ; Fourier transform infrared spectroscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract κ-Casein as purified from bovine milk exhibits a rather unique disulfide bonding pattern as revealed by SDS-PAGE. The disulfide-bonded caseins present range from dimer to octamer and above and preparations contain about 10% monomer. All of these heterogenous polymers, however, self-associated into nearly spherical uniform particles with an average radius of 8.9 nm as revealed by negatively stained transmission electron micrographs. Evidence is presented that multivalent cations play a role in the stabilization of these spherical particles. Treatment with EDTA causes disruption of theκ-casein particles and leads to a broader size distribution as judged by electron microscopy and dynamic light scattering. The size and shape of the particles are in accord with earlier proposed 3D models forκ-casein that actually predicted participation of divalent cations in the structure.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part B: Polymer Physics 36 (1998), S. 805-813 
    ISSN: 0887-6266
    Keywords: collagen ; surfactants ; calorimetry ; segment-long-spacing ; anionic ; titration ; sodium lauryl sulfate ; castor oil ; Physics ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Leather, a textile based on collagen, usually requires the addition of sulfated oils that have been recently found to cause instability when heated in critical manufacturing processes. Here reactions between collagen and sodium dodecyl sulfate (SDS), sulfated castor oil, or a synthetic sulfated oil are studied calorimetrically. Sodium lauryl sulfate below its critical micelle concentration (cmc) displayed an immediate exotherm due to equilibrium binding of the reagents with stoichiometry n = 12.6 ± 0.2, K = (2.02 ± 0.8) × 107 M-1, and enthalpy ΔH = 62 ± 2 Kcal/mol; and a delayed endotherm due to denaturation of collagen. The endotherms accompanying the reactions with sulfated oils with longer chains were smaller, with no apparent denaturation of collagen. The micellar nature of these surfactants was apparent from very large n for sulfated castor oil, 4082 ± 11 and a very small value of ΔH, 0.77 ± 0.01 cal/mol. The binding of sulfated castor oil at the polar bands of collagen crystallites, comprising extended molecules arranged side-by-side, was shown directly by electron microscopy. © 1998 John Wiley & Sons, Inc. J Polym Sci B: Polym Phys 36: 805-813, 1998
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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