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J. Biol. Chem., Vol. 266, Issue 7, 4168-4172, 03, 1991
A Kurosaka, A Yano, N Itoh, Y Kuroda, T Nakagawa and T Kawasaki
Antiserum raised against horseradish peroxidase (HRP) recognizes a neural
specific carbohydrate antigen in Drosophila and other insects. The epitopic
activity of the carbohydrate moiety of HRP recognized by anti-HRP antiserum
was measured by a newly developed enzyme-linked immunosorbent assay, in
which HRP glycopeptides conjugated with bovine serum albumin were coated
onto the wells and then reacted with goat anti-HRP antiserum. HRP sugar
moieties released by almond glycopeptidase A digestion of HRP pepsin
digests were subjected to pyridylamination. Pyridylamino oligosaccharides
were separated into seven fractions by reverse-phase high performance
liquid chromatography. The major fraction, which comprised about 80% of the
total sugars, reacted strongly with anti-HRP antiserum. The carbohydrate
structure of this fraction was determined by sugar composition analysis and
600-MHz 1H NMR spectroscopy as follows: Man alpha 1----6(Man alpha
1----3)(Xyl beta 1----2)Man beta 1----4GlcNAc beta 1----4(Fuc alpha
1----3)GlcNAc. Analyses of reactivity with anti- HRP antiserum of various
oligosaccharide derivatives obtained from the major fraction by
exoglycosidase digestion and partial acid hydrolysis indicated that alpha
1----6-linked mannose and alpha 1----3-linked fucose are predominantly
involved in the epitopic structure.
The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum
Department of Biotechnology, Faculty of Engineering, Sangyo University, Japan.
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