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  • γ-Carboxyglutamic Acid  (2)
  • Calciphylaxis  (1)
  • Calcium  (1)
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  • 1
    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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  • 2
    Electronic Resource
    Electronic Resource
    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
    Keywords: 31P NMR spectroscopy ; Phosphoprotein ; Dentin ; Calcium ; Inorganic orthophosphate ; Bovine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405129
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  • 3
    Electronic Resource
    Electronic Resource
    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
    Keywords: Calcification ; Calciphylaxis ; Skin ; Serine Phosphate ; Threonine Phosphate ; γ-Carboxyglutamic Acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02409434
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