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(Received for publication, November 14, 1994) The CD52 antigen was extracted from human spleens with organic
solvents and purified by immunoaffinity and reverse-phase
chromatography. The latter step resolved two CD52 species, called
CD52-I and CD52-II. Both species were found to contain similar N-linked oligosaccharides and glycosylphosphatidylinositol
(GPI) anchor glycans. The N-linked oligosaccharides were
characterized by methylation linkage analysis and, following exhaustive
neuraminidase and endo- The difference
between CD52-I and CD52-II was in the phosphatidylinositol (PI)
moieties of the GPI anchors. The phosphatidylinositol-specific
phospholipase C-sensitive CD52-I contained exclusively distearoyl-PI,
while the PI-phospholipase C-resistant CD52-II contained predominantly
a palmitoylated stearoyl-arachidonoyl-PI, as judged by electrospray
ionization mass spectrometry. Tandem mass spectrometric studies
indicated that the palmitoyl residue of the CD52-II anchor is attached
to the 2-position of the myo-inositol ring. Both the CD52-I
and CD52-II PI structures are unusual for GPI anchors and the possible
significance of this is discussed. The alkali-lability of the CD52
epitope recognized by the Campath-1H monoclonal antibody was studied.
The data suggest that the alkali-labile hydroxyester-linked fatty acids
of the GPI anchor are necessary for antibody binding.
Volume 270,
Number 11,
Issue of March 17, 1995 pp. 6088-6099
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-galactosidase digestion, by the reagent
array analysis method
. The results showed that the single
CD52 N-glycosylation site is occupied by large sialylated,
polylactosamine-containing, core-fucosylated tetraantennary
oligosaccharides. The locations of the phosphoryl substituents on the
GPI anchor glycan were determined using a new and sensitive method
based upon partial acid hydrolysis of the GPI glycan.
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