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  • γ-Carboxyglutamic Acid  (2)
  • 31P-NMR  (1)
  • Amorphous calcium phosphate  (1)
  • 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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    Paper (German National Licenses)
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  • 2
    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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    Paper (German National Licenses)
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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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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Failure to detect an amorphous calcium-phosphate solid phase in bone mineral: A radial distribution function study (1984)
    Springer
    Calcified tissue international 36 (1984), S. 291-301 
    Details
    ISSN: 1432-0827
    Keywords: Bone ; Mineral ; Amorphous calcium phosphate ; X-ray diffraction ; Radial distribution function
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary X-ray diffraction radial distribution function analysis was used to determine if a significant amount of an amorphous solid phase of calcium phosphate exists in bone, and if so, whether the amount varies as a function of age and maturation. Unfractionated cortical bone from embryonic and posthatch chicks of various ages and a low-density fraction of embryonic bone were studied. No evidence was found for the presence of an amorphous solid phase of calcium phosphate in any of the samples studied, including the recently deposited bone mineral of the low density fraction of embryonic bone. As little as 12.5% of synthetic amorphous calcium phosphate (ACP) added to bone was readily detected by the radial distribution function technique used. The results clearly indicate that the concept that ACP is the initial solid mineral phase deposited in bone, and the major mineral constituent of young bone is no longer tenable. The concept does not provide an accurate description of the nature of the initial bone mineral deposited, or the changes that occur with maturation, nor can it acount for the compositional and X-ray diffraction changes that the mineral component undergoes during maturation and aging.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405333
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    Paper (German National Licenses)
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