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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 56 (1995), S. 323-330 
    ISSN: 1432-0827
    Keywords: Porcine secretory enamel ; Porcine 32 kDa enamelin ; Asparagine-linked oligosaccharide ; Pyridylamination ; Sequential exoglycosidase digestion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract The structures of asparagine-linked oligosaccharides of porcine 32 kDa enamelin are reported. The oligosaccharides were released by N-oligosaccharide glycopeptidase digestion, and the reducing ends of the oligosaccharides were derivatized with a fluorescent reagent, 2-aminopyridine. The pyridylamino oligosaccharides were separated into eight kinds of oligosaccharides. The structures of these oligosaccharides were determined by a combination of a sequential exoglycosidase digestion and a two-dimensional suger mapping technique. The oligosaccharides consisted of fucose, galactose, mannose, N-acetylglucosamine, and N-acetylneuraminic acid, and were classified into two groups according to their core-sugar chain structures; one was a biantennary-type and the other was a triantennary-type oligosaccharide. The variation of the oligosaccharides in each of these groups was caused by the differences in the number, the site, and the mode of linkage of N-acetylneuraminic acid to the core-sugar chains.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 54 (1994), S. 69-75 
    ISSN: 1432-0827
    Keywords: Porcine secretory enamel ; Porcine amelogenin ; Plasma desorption mass spectometry ; Amino acid sequence ; CNBr cleavage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Amelogenins were extracted from the thin outer layer of porcine secretory enamel and purified by gel filtration and reverse-phase HPLC. The results of amino acid sequencing of the purified porcine amelogenins indicated the presence of at least four prototype amelogenins translated from alternatively spliced transcripts. The results of mass spectroscopy of the CNBr-cleaved peptides derived from the 25kDa amelogenin indicated that porcine 25kDa amelogenin is neither phosphorylated nor glycosylated.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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