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  • 1
    Electronic Resource
    Electronic Resource
    Purification, composition, and31P NMR spectroscopic properties of a noncollagenous phosphoprotein isolated from chicken bone matrix (1981)
    Springer
    Calcified tissue international 33 (1981), S. 385-394 
    Details
    ISSN: 1432-0827
    Keywords: Phosphoprotein ; Bone ; 31P-NMR ; Phosphoserine ; Phosphothreonine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Fractionation of the EDTA-soluble, noncollagenous proteins of the organic matrix of chicken bone by Sephadex G-100 molecular sieving has revealed that the majority of the organic phosphorus is present in two fractions, from one of which a homogeneous phosphoprotein has been isolated. The purified phosphoprotein has an apparent molecular weight of 12,000 and contains bothO-phosphoserine andO-phosphothreonine.31P-NMR spectroscopy demonstrates that all of the organic phosphorus exists in the form of phosphomonoesters which have an average pK2 of 6.8. The phosphoprotein is highly acidic due to its high content of dicarboxylic acids in addition to the presence of organic phosphorus. The characteristic amino acid composition of the phosphoprotein establishes its noncollagenous nature and highlights the differences among bone, dentin, and enamel phosphoproteins. The absence ofγ-carboxyglutamic acid distinguishes it from osteocalcin, the noncollagenousγ-carboxyglutamic acid-containing peptide of bone matrix.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02409461
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of phosphopeptides andγ-carboxyglutamic acid-containing peptides in epiphyseal growth plate cartilage (1979)
    Springer
    Calcified tissue international 27 (1979), S. 187-191 
    Details
    ISSN: 1432-0827
    Keywords: Phosphopeptides ; γ-Carboxyglutamic Acid ; Calcified Cartilage ; Phosphoserine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Uncalcified cartilage from the epiphyseal portion of bovine scapulae, both distant and adjacent to the epiphyseal growth plate, and the calcified cartilage of the epiphyseal growth plate itself were analyzed for the presence of O-phosphoserine [Ser(P)], O-phosphothreonine [Thr(P)] and γ-carboxyglutamic acid (Gla). Only trace amounts of these Ca2+-binding amino acids or the peptides containing them were found in the unmineralized tissues. In contrast, whole calcified cartilage, and especially the most mineralized fraction obtained by density centrifugation, contained considerable amounts of all three amino acids. Essentially all of the Gla and the majority of the Ser(P) and Thr(P) were present in non-collagenous, non-diffusible proteins extractable in EDTA at near-neutral pH.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02441183
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