Sandbox Reserved 703: Difference between revisions
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HPBP is associated in vivo with PON1, and binds inorganic phosphate ions.<ref>PMID:16511265</ref> During research, it was possible to show that the separation of HPBP and PON1 involves a fast denaturing of the two proteins, which means that the PON1/HPBP complex is essential for each other’s stability. | HPBP is associated in vivo with PON1, and binds inorganic phosphate ions.<ref>PMID:16511265</ref> During research, it was possible to show that the separation of HPBP and PON1 involves a fast denaturing of the two proteins, which means that the PON1/HPBP complex is essential for each other’s stability. | ||
The different oligomeric organisations of the PON1/HPBP complex depend on the calcium, phosphate and detergent concentrations. Therefore, this complex is implicated in the phosphocalcic metabolism. Normally, the phosphate concentration should always be around 0.5-1.0 mM, hence HPBP is always saturated with phosphate. | The different oligomeric organisations of the PON1/HPBP complex depend on the calcium, phosphate and detergent concentrations. Therefore, this complex is implicated in the phosphocalcic metabolism. Normally, the phosphate concentration should always be around 0.5-1.0 mM, hence HPBP is always saturated with phosphate. | ||
The existence of a phosphate detector in human plasma, associated with a lipoprotein, demonstrate the necessity to avoid the direct contact between phosphate and calcium. Indeed, hyperphosphatemia is a risk factor for cardio vascular diseases.<ref>PMID:17556053</ref> | The existence of a phosphate detector in human plasma, associated with a lipoprotein, demonstrate the necessity to avoid the direct contact between phosphate and calcium. Indeed, hyperphosphatemia is a risk factor for cardio vascular diseases.<ref>PMID:17556053</ref><ref>PMID:18031277</ref> | ||
== '''Structure''' == | == '''Structure''' == | ||