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  • 1
    Electronic Resource
    Electronic Resource
    Influence of Neutral Salts on the Hydrothermal Stability of Acid-Soluble Collagen (2000)
    Springer
    The protein journal 19 (2000), S. 85-92 
    Details
    ISSN: 1573-4943
    Keywords: Soluble collagen ; thermal stability ; NaCl ; KCl
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The thermal stability of acid-soluble collagens was studied by circular dichroism (CD) spectroscopy. Adult bovine dermal collagen (BDC), rat-tail tendon collagen (RTC), and calf skin collagen (CSC) were compared. Despite some variability in amino acid composition and apparent molecular weight, the CD spectra for helical and unordered collagen structures were essentially the same for all the sources. The melting of these collagens occurs as a two-stage process characterized by a pretransition (T p) followed by complete denaturation (T d). The characteristic temperatures vary with the source of the collagen; for mature collagens (BDC, RTC) T p = 30°C and T d = 36deg;C, and for CSC T p = 34°C and T d = 40°C. Neutral salts, NaCl or KCl, at low concentrations (0.02–0.2 M) appear to bind to the collagens and shift the thermal transitions of these collagens to lower temperatures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007074314686
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Particle sizes of purified κ-casein: Metal effect and correspondence with predicted three-dimensional molecular models (1996)
    Springer
    The protein journal 15 (1996), S. 435-445 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF01886850
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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