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  • Bone  (4)
  • Springer  (4)
  • American Geophysical Union (AGU)
  • 2000-2004
  • 1975-1979  (4)
  • 1
    Electronic Resource
    Electronic Resource
    Preliminary studies on the binding of plasma albumin to bone tissue (1977)
    Springer
    Calcified tissue international 23 (1977), S. 303-305 
    Details
    ISSN: 1432-0827
    Keywords: Albumin ; Bone ; Hydroxyapatite ; Plasma protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The extractability of125I-labelled plasma albumin from bone pieces and from powdered bone has been compared after both in vivo and in vitro incorporation. The results show that albumin is more readily extracted from bone pieces than from bone powder which implies that tissue disruption exposes additional protein adsorption sites. It is suggested that incorporation of plasma albumin into calcified matrix during bone formation occurs mainly as a result of its strong interaction with bone mineral.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02012801
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  • 2
    Electronic Resource
    Electronic Resource
    Plasma disappearance of rabbit α2 HS-glycoprotein and its uptake by bone tissue (1978)
    Springer
    Calcified tissue international 26 (1978), S. 155-161 
    Details
    ISSN: 1432-0827
    Keywords: Plasma protein ; Glycoprotein ; Bone ; Glucosamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Plasmaα 2HS-glycoprotein is specifically accumulated in calcified tissues. In the present studies this glycoprotein was isolated from plasma and after iodination with iodine-125 was injected intravenously into young rabbits. The tissue distribution and plasma disappearance rate of this radioactively labeled material were determined. Of the various tissues studied, bone showed the greatest retention of labeled glycoprotein expressed as percentage of the injected dose per gram tissue relative to the plasma content. The rate of loss of iodinatedα 2HS-glycoprotein from plasma was similar to that ofα 2HS-glycoprotein labeled endogenously by using14C-glucosamine or3H-glucosamine. The uptake of exogenously labeled3I-α 2HS-glycoprotein into bone tissue expressed as a percentage of the injected dose was similar to that of endogenously labeled14C-α 2HS-glycoprotein. These results suggest that the125I-labeled material can be used to study further the metabolism ofα 2HS-glycoprotein by bone tissue.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02013251
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  • 3
    Electronic Resource
    Electronic Resource
    Plasma proteins present in human cortical bone: Enrichment of theαHS-glycoprotein (1977)
    Springer
    Calcified tissue international 22 (1977), S. 27-33 
    Details
    ISSN: 1432-0827
    Keywords: Protein ; Bone ; Blood plasma ; Dentine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract The spectrum of plasma proteins present in human cortical bone and permanent dentine has been determined. One plasma glycoprotein, theαHS-glycoprotein, was found to be present at a high concentration in both bone and dentine and was shown to be concentrated in the mineralized tissues with respect to the other plasma proteins by factors of between 30 and 100. In this respect theαHS-glycoprotein is analogous to the G2B-glycoprotein and α-glycoprotein of bovine and rabbit b one, respectively. The binding ofαHS-glycoprotein and albumin to calcium phosphates generated within serum samples has been studied at different serum: precipitate ratios. In each case all theαHS-glycoprotein was removed from the samples and theαHS-glycoprotein was concentrated with respect to albumin by factors ranging from 370 at the highest serum: precipitate ratio to 25 at the lowest ratio. The plasmaαHS-glycoprotein concentrations of patients with Paget's disease of bone were shown to be substantially lower than the normal range, with significant negative correlation between theαHS-glycoprotein concentration and the plasma alkaline phosphatase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02010343
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  • 4
    Electronic Resource
    Electronic Resource
    Movement of125I albumin and125I polyvinylpyrrolidone through bone tissue fluid (1977)
    Springer
    Calcified tissue international 23 (1977), S. 103-112 
    Details
    ISSN: 1432-0827
    Keywords: Albumin ; Polyvinylpyrrolidone ; Tissue fluid ; Bone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The passage of tissue fluid through cortical bone has been investigated using radioactively labelled macromolecules as markers. The results suggest that in the cortex of young rabbit femur the movement of tissue fluid is in the same net direction as blood, mainly from the endosteal to the periosteal surface. Some albumin is incorporated from extravascular tissue fluid into calcified matrix at sites of bone formation. Polyvinylpyrrolidone, average molecular weight 35,000 is able to pass through extravascular tissue fluid in bone but isnot incorporated into calcified matrix. In rabbits made vitamin D deficient, much less albumin is retained in regions of bone formation than is the case with controls. Albumin adsorbs to the surface of calcium phosphate precipitates and it is suggested that this mechanism may be mainly responsible for its incorporation into bone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02012773
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