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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 30 (1980), S. 167-174 
    ISSN: 1432-0827
    Keywords: Proteolipid ; Calcium-phospholipid-phosphate complexes ; Calcification ; Hydroxyapatite ; Membranes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Calcium-phospholipid-phosphate complexes (Ca-PL-P) were isolated from calcified and uncalcifiedBacterionema matruchotii and its calcified lipid extracts. Similar complexes were absent from the noncalcifying bacteriumActinomyces naeslundii. The majority of the Ca-PL-P complexes were associated with the proteolipid acidic phospholipid component. Ca-PL-P complexes isolated fromB. matruchotii and from calcified proteolipid contained phosphatidylinositol, phosphatidylinositol-4-phosphate, phosphatidylinositol-4,5-diphosphate, and phosphatidylserine. They consisted of approximately 52 mole % Ca, 32 mole % organic P, and 15 mole % Pi. During Ca-PL-P extraction fromB. matruchotii or its proteolipid-containing calcified lipid extracts, the proteolipid was dissociated and the apoprotein precipitated as fluff at the aqueous-organic solvent interface, thus explaining the failure to detect protein in Ca-PL-P preparations. When the ability of Ca-PL-P complexes and lipid fractions ofB. matruchotii to initiate apatite formation from metastable calcium phosphate solution was compared, the yield of hydroxyapatite decreased as follows: Ca-PL-P 〉 proteolipid acidic phospholipids 〉 proteolipid 〉 crude phospholipid 〉 total lipids 〉 whole cells.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 36 (1984), S. 214-218 
    ISSN: 1432-0827
    Keywords: Proteolipid ; Calcium-phospholipid-phosphate complexes ; Calcification ; Hydroxyapatite ; Membranes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary This study demonstrates that calciumphospholipid-phosphate complexes (CPLX) and calcifiable proteolipid are associatedin vivo by establishing that they can be co-isolated from calcified bacteria. Both of these membrane constituents, which support apatite formationin vitro, have been isolated independently fromBacterionema matruchotii. However, isolation of proteolipid was preceded by demineralization in 2N formic acid, thereby dissociating bound Ca, whereas isolation of CPLX included sonication of calcified bacteria in 2:1:1.5 chloroform:methanol:Tris buffer, thereby dissociating any protein. Co-isolation is possible by demineralizing the calcified bacteria with 50 mM phthalic acid, pH 5.5, followed by extraction with 2:1 chloroform:methanol, and precipitation of crude phospholipid with acetone. CPLX and proteolipid are present in all Sephadex LH-20 chromatographic fractions of the crude phospholipid and of diethyl ether precipitates of the crude phospholipid. CPLXs contain protein:phospholipid:Ca:Pi but differ in relative composition from each other and from independently isolated CPLX. The Ca:phospholipid:Pi molar ratio of diethyl ether precipitable proteolipid-CPLX is most similar to previously published values for CPLX. The protein content of CPLX accounts for all of the proteolipid apoprotein in each Sephadex LH-20 fraction.
    Type of Medium: Electronic Resource
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