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  • 1980-1984  (3)
  • Phosphoprotein  (2)
  • Skin  (1)
  • 1
    Digitale Medien
    Digitale Medien
    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
    Schlagwort(e): Phosphoprotein ; Bone ; 31P-NMR ; Phosphoserine ; Phosphothreonine
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin , Physik
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02409461
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Serine phosphate, threonine phosphate and γ-carboxyglutamic acid in normal and experimentally induced, pathologically calcified rat skin (topical cutaneous calciphylaxis) (1981)
    Springer
    Calcified tissue international 33 (1981), S. 185-188 
    Details
    ISSN: 1432-0827
    Schlagwort(e): Calcification ; Calciphylaxis ; Skin ; Serine Phosphate ; Threonine Phosphate ; γ-Carboxyglutamic Acid
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin , Physik
    Notizen: Summary The amount of non-collagenous proteins is increased greatly during the pathological calcification of rat skin experimentally induced by dihydrotachysterol (DHT) and Ovalbumin (topical cutaneous calciphylaxis). This is accompanied by an increase in the total amount and concentrations of protein-bound serine phosphate [Ser(P)], threonine phosphate [Thr(P)] and γ-carboxyglutamic acid (Gla), almost all of which can be extracted from the tissue and can be dissociated from collagen in 0.5M EDTA. The EDTA-soluble, non-collagenous proteins are rich in aspartic and glutamic acids, similar to the non-collagenous, EDTA-soluble proteins of bone, cementum and calcified cartilage, and quite distinct from those of dentin and enamel.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02409434
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  • 3
    Digitale Medien
    Digitale Medien
    31P nuclear magnetic resonance spectroscopic evidence for ternary complex formation of fetal dentin phosphoprotein with calcium and inorganic orthophosphate ions (1983)
    Springer
    Calcified tissue international 35 (1983), S. 815-818 
    Details
    ISSN: 1432-0827
    Schlagwort(e): 31P NMR spectroscopy ; Phosphoprotein ; Dentin ; Calcium ; Inorganic orthophosphate ; Bovine
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin , Physik
    Notizen: Summary The single phosphoprotein of fetal calf dentin, having a molecular weight of approximately 94,000 and a phosphorus content of 8% (w/w), was examined by31P NMR spectroscopy. The single resonance at 3.7 ppm at pH 10 and its chemical shift during acid titration established the phosphomonoester nature of the organic phosphorus moiety. During titration of the phosphoprotein with CaCl2 in the presence of inorganic orthophosphate ions, line broadening for the orthophosphate resonance was both phosphoprotein- and calcium-dependent, indicating ternary complex formation. The data indicate that the phosphoprotein of fetal calf dentin binds both calcium and inorganic orthophosphate ions and therefore has the requisite physical chemical properties necessary for it to facilitate the heterogeneous nucleation of a Ca-PO4 solid phase from solution during tissue mineralization.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02405129
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