The main mineral constituent of bone and teeth

Herman, H; Dallemagne, M. J.

doi:10.1016/0003-9969(61)90007-3

Cited by 32 publications

(10 citation statements)

References 2 publications

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“…Further evidence for HPO42-groups in CO3-free, Ca-deficient HA is giv-0171-967X/81/0033-0111 $01.40 en by the presence of HPO42-infrared absorption bands which are absent in stoichiometric HA [1]. It should be noted that heating bone to 300-400~ results in the formation of significant amounts of PzO74- [9], supporting the view that bone apatite is Ca deficient. This paper reports on the formation of Cadeficient HA by allowing amorphous calcium phosphate (ACP) to transform to HA in a series of aqueous slurries of different concentrations.…”

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confidence: 84%

Formation and structure of Ca-deficient hydroxyapatite

1981

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When amorphous calcium phosphate (ACP) was transformed to crystalline hydroxyapatite (HA) in a series of aqueous slurry concentrations ranging from low to high, the higher slurry concentrations produced more Ca-deficient HA as measured by Ca/P ratio and heat-produced pyrophosphate. We feel that the excess solution phosphate produced in the higher slurry transformations results in lower Ca/P ratio HA. It has been suggested that an ACP is the precursor to bone apatite. Regulation of the in vivo ACP slurry concentration could then control the stoichiometry and, therefore, the metabolic activity of bone apatite. X-ray radial distribution function (RDF) analyses showed that CO3(2-) substitution in HA creates far greater structural distortions than do Ca deficiencies. The latter, however, do produce small, but observable, structural distortions when compared to stoichiometric HA. It now seems clear that the RDF of bone apatite can be modeled by a synthetic, Ca-deficient, CO3(2-)-containing HA.

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confidence: 84%

Formation and structure of Ca-deficient hydroxyapatite

1981

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“…[The true dry weight of native whole bone is difficult to determine very accurately because of the presence of bound water, which is not wholly released except at very high temperatures (Francois & Herman, 1961;Herman & Dallemagne, 1961 Presence ofalkali-stable phospho amino acids and of hexose phosphates. Samples of proteins were hydrolysed in 3M-KOH for 3h at 100°C in sealed glass tubes.…”

Section: Analytical Determinationsmentioning

confidence: 99%

“…Samples of the freshly dissected and cleaned bone were dried at room temperature in a vacuum desiccator until a constant weight was achieved, and then ashed at 600'C for 18-20 h. Another sample of freshly dissected and cleaned bone was dried in an oven at 105°C until a constant weight was achieved (usually 4-6h), and similarly ashed at 600°C for 18-24h. [The true dry weight of native whole bone is difficult to determine very accurately because of the presence of bound water, which is not wholly released except at very high temperatures (Francois & Herman, 1961;Herman & Dallemagne, 1961 (Clark & Collip, 1925) and total phosphorus (Chen et al, 1956) Grant (1964). The hydrolysates were either analysed directly or after precipitation of most of the calcium and phosphorus by adjusting the pH (Glimcher & Levine, 1966 Chen et al (1956).…”

Section: Analytical Determinationsmentioning

confidence: 99%

Identification of organic phosphorus covalently bound to collagen and non-collagenous proteins of chicken-bone matrix. The presence of O-phosphoserine and O-phosphothreonine in non-collagenous proteins, and their absence from phosphorylated collagen

Cohen-Solal

Lian

Kossiva

et al. 1979

Biochemical Journal

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Non-collagenous phosphoproteins, almost all of which can be extracted in EDTA at neutral pH in the presence of proteinase inhibitors, are identified in the matrix of chicken bone, and are therefore not covalently bound to collagen. Similarly, all the peptides containing y-carboxyglutamic acid are present in the EDTA extract and none in the insoluble residue, confirming that none is covalently linked to chicken bone collagen. However, organic phosphorus is also found to be present in chicken bone collagen, principally in the a2-chains. Of the total protein-bound organic phosphorus present in chicken bone matrix, approx. 80 % is associated with the non-collagenous proteins and 20 % with collagen. The soluble non-collagenous proteins contain both O-phosphoserine and 0-phosphothreonine and these account for essentially all of their organic phosphorus content. In contrast, collagen contains neither 0-phosphoserine nor 0-phosphothreonine. Indeed, no phosphorylated hydroxy amino acid, phosphoamidated amino acid or phosphorylated sugar could be identified in purified components of collagen, which contain approximately four to five atoms of organic phosphorus per molecule of collagen. Peptides containing organic phosphorus were isolated from partial acid hydrolysates and enzymic digests of purified collagen components, which contain an as-yet-unidentified cationic amino acid. These data, the very high concentrations of glutamic acid in the phosphorylated peptides, and the pH-stability of the organic phosphorus moiety in intact collagen chains strongly suggest that at least part of the organic phosphorus in collagen is present as phosphorylated glutamic acid. This would indicate that the two major chemically different protein fractions in chicken bone matrix that contain organic phosphorus may represent two distinct metabolic pools of organic phosphorus under separate biological control.Phosphoproteins have been identified as part of the non-collagenous components of the organic matrices of mineralized vertebrate tissues such as enamel (Seyer & Glimcher, 1971;Papas et al., 1977;Seyer & Glimcher, 1977a), dentine Veis & Perry, 1967;Butler, 1972;Butler et al., 1972;Veis et al., 1972;Carmichael & Dodd, 1973;Pieri et al., 1975;Menanteau et al., 1977) and bone (Spector & Glimcher, 1972;Shuttleworth & Veis, 1972) [see Leaver et al. (1975b) for a review]. There still exists, however, at least two major points of controversy with regard to bone and dentine: (1) how much, if any, of the phosphorylated protein(s) is covalently bound to the collagen, and (2), if present, Abbreviation used: P,, organic phosphate. * Present address: I.N.S.E.R.M. U12 and U18, Hc6pital des Enfants malades, Paris, France. t To whom requests for reprints should be addressed. Vol. 177 the nature of the organic phosphate moiety covalently bound to the collagen.Although evidence has been presented that none of the phosphoprotein is covalently bound to the collagen of rat dentine (Butler, 1972;Butler et al., 1972Butler et al., , 1976, equally substantia...

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“…Acid phosphate in normal tooth enamel converts to pyrophosphate (P2074 ) between -300 and 600~ [33,34]; the pyrophosphate formed reacts at higher temperature, -650-700~ with a portion of the apatite phase to form [3-TCP [33].…”

Section: Discussionmentioning

confidence: 99%

Compositional, structural, and phase changes inin vitro laser-irradiated human tooth enamel

1984

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Tooth enamel laser irradiated under certain conditions previously has been shown to have reduced subsurface demineralization rates. Identification of these laser-induced changes has bearing on understanding the dissolution rate reduction mechanism; some of these changes, ones that occur in high temperature regions, were studied in this report. X-ray diffraction and infrared spectroscopy were used to identify changes in enamel of extracted intact human teeth subjected to high energy density (approximately 10,000 J/cm2) 10.6 microns wavelength carbon dioxide laser irradiance. The laser irradiance melted the enamel apatite; this solidified melt was composed of minor phases of alpha-tricalcium phosphate, alpha-Ca3 (PO4)2, and tetracalcium phosphate, Ca4(PO4)2O, and a major phase of modified apatite. The apatite modifications, as compared with the original were (1) reductions in contents of water, protein, carbonate, and chloride (or chloride rearrangement); (2) essentially no change in apatite hydroxide content; (3) possible incorporation of oxide replacing some hydroxide ions; and (4) an uptake of traces of carbon dioxide and cyanate. An infrared band at 434 cm-1 that appears in spectra of hydroxyapatite partially dehydroxylated by thermal treatment was assigned to oxide translation. This band was utilized to search for oxide formation in the laser-irradiated tooth enamel.

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The main mineral constituent of bone and teeth

Cited by 32 publications

References 2 publications

Formation and structure of Ca-deficient hydroxyapatite

Formation and structure of Ca-deficient hydroxyapatite

Identification of organic phosphorus covalently bound to collagen and non-collagenous proteins of chicken-bone matrix. The presence of O-phosphoserine and O-phosphothreonine in non-collagenous proteins, and their absence from phosphorylated collagen

Compositional, structural, and phase changes inin vitro laser-irradiated human tooth enamel

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