Structure of the glycosylphosphatidylinositol membrane anchor of human placental alkaline phosphatase
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چکیده
منابع مشابه
Structure of the glycosylphosphatidylinositol membrane anchor of human placental alkaline phosphatase.
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 deaminatio...
متن کاملThe Glycosylphosphatidylinositol Anchor: A Complex Membrane-Anchoring Structure for Proteins†
Positioned at the C-terminus of many eukaryotic proteins, the glycosylphosphatidylinositol (GPI) anchor is a posttranslational modification that anchors the modified protein in the outer leaflet of the cell membrane. The GPI anchor is a complex structure comprising a phosphoethanolamine linker, glycan core, and phospholipid tail. GPI-anchored proteins are structurally and functionally diverse a...
متن کاملPhospholipase resistance of the glycosyl-phosphatidylinositol membrane anchor on human alkaline phosphatase.
Alkaline phosphatase (ALP) is attached to the cell surface in mammalian tissues via a glycosyl-phosphatidylinositol (GPI) anchor and can be released from the membrane by GPI-specific phospholipases. In a range of cultured human cell lines, however, the sensitivity of ALP to phospholipases was observed to be variable in magnitude (approximately 20-90%). The mechanism of phospholipase resistance ...
متن کاملChemical characterization of the membrane-anchoring domain of human placental alkaline phosphatase.
Membrane and soluble forms of alkaline phosphatase (ALP) were selectively prepared from human placental microsomes by treatment with 1-butanol at pH 8.5 and 5.5, respectively. The purified membrane (mALP) and soluble (sALP) forms were analyzed for chemical compositions. mALP was found to contain 1 mol each of palmitate, stearate, and glycerol/subunit of ALP, which were absent in sALP. Both the ...
متن کاملNucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase.
A cDNA clone for human adult intestinal alkaline phosphatase (ALP) [orthophosphoric-monoester phosphohydrolase (alkaline optimum); EC 3.1.3.1] was isolated from a lambda gt11 expression library. The cDNA insert of this clone is 2513 base pairs in length and contains an open reading frame that encodes a 528-amino acid polypeptide. This deduced polypeptide contains the first 40 amino acids of hum...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1994
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3020861