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Last Updated: 3 years ago

Possible Interaction: Alkaline Phosphatase and Phosphatidylethanolamine

Research Papers that Mention the Interaction

Human skeletal ALP extracted from bone was inhibited by cephalin , but the skeletal isoenzyme in Pagetic serum was not, suggesting that the potential for phospholipid interaction was altered during or after release from osteoblast cell membranes.
Like the extracted human isoenzyme, the extracted chick ALP was subject to competitive inhibition by cephalin (Ki = 0.3 mM at pH 9.3) and an inhibitory interaction between cephalin and imidazole, but the same isoenzyme showed neither effect in situ.
Archives of biochemistry and biophysics  •  1983  |  View Paper
Biochemically, the reduction in ALP activity is associated with alterations in the extracellular metabolism of various phosphorylated compounds, including inorganic pyrophosphate (PPi), phosphoethanolamine , and pyridoxal 5'-phosphate.
Critical reviews in clinical laboratory sciences  •  1991  |  View Paper
Unbalanced phospholipid composition due to depletion of the major phospholipid of Escherichia coli, phosphatidylethanolamine , was shown previously to significantly decrease the secretion and transcriptional expression of periplasmic alkaline phosphatase of this bacterium.
Biochemistry (Moscow)  •  2004  |  View Paper
It has been shown that the effect of phosphatidylethanolamine but not anionic phospholipids on the efficiency of alkaline phosphatase secretion is determined by the primary structure of its N-terminal region.
The absence of phosphatidylethanolamine appreciably reduces the efficiency of secretion of wild type alkaline phosphatase and its mutant forms with amino acid substitutions in positions +5+6 and +13+14.
Biochemistry (Moscow)  •  2004  |  View Paper