Abstract
EARLIER we suggested a role for matrix-bound organic phosphorus in the initiation of mineralization. The evidence supporting our hypothesis was provided by observations on the interaction of collagen and inorganic orthophosphate in vitro1,2 and the finding of small amounts of protein-bound organic phosphorus in purified collagens and gelatines and the single stranded α chains from a number of different soft tissues from different animals3. The content of organic phosphorus was found to be considerably higher in the organic matrix proteins of embryonic and adult dental enamel, in which serine phosphate bound to protein was identified4. Enzymes which catalysed a phosphoryl transfer from adenosine triphosphate5 to enamel proteins, in addition to collagens and gelatines6, were also characterized.
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FRANCOIS, C., GLIMCHER, M. & KRANE, S. Organic Phosphorus Content of the Alpha Chains of Chicken Bone Collagen. Nature 214, 621–622 (1967). https://doi.org/10.1038/214621a0
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DOI: https://doi.org/10.1038/214621a0
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