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. 1994 Sep 15;302(Pt 3):861–865. doi: 10.1042/bj3020861

Structure of the glycosylphosphatidylinositol membrane anchor of human placental alkaline phosphatase.

C A Redman 1, J E Thomas-Oates 1, S Ogata 1, Y Ikehara 1, M A Ferguson 1
PMCID: PMC1137310  PMID: 7945214

Abstract

The glycosylphosphatidylinositol membrane anchor of human placental alkaline phosphatase was isolated by exhaustive proteolysis followed by hydrophobic interaction chromatography. The resulting glycosylphosphatidylinositol-peptide was subjected to compositional analysis and chemical and enzymic modifications. The neutral-glycan fraction, prepared by dephosphorylation followed by HNO2 deamination and reduction, was sequenced using exoglycosidases and acetolysis. The phosphatidylinositol moiety was analysed by fast-atom bombardment mass spectrometry and gas chromatography-mass spectrometry. Taken together the data suggest the structure, Thr-Asp-ethanolamine-PO4-Man alpha 1-2Man alpha 1-6Man alpha 1-4GlcN-(sn-1-O- alkyl-2-O-acylglycerol-3-PO4-1-myo-D-inositol), which contains an additional ethanolamine phosphate group at an unknown position.

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Selected References

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