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pubmed-article:1904864pubmed:issue18lld:pubmed
pubmed-article:1904864pubmed:dateCreated1991-7-24lld:pubmed
pubmed-article:1904864pubmed:abstractTextThe mucin-type sugar chains of human milk galactosyltransferase samples purified from two donors with different blood types were released by alkaline borohydride treatment and quantitatively labeled by N-[3H]acetylation. The radioactive oligosaccharides thus obtained were fractionated by high performance liquid chromatography and immobilized lectin chromatography, and their structures were studied by sequential digestion with endo- or exoglycosidases, methylation analysis, and periodate oxidation. It was revealed that the structures of the mucin-type sugar chains of galactosyltransferase are extremely various, and many blood group determinants are expressed on more than 13 different backbone sugar chains. The characteristic features of the sugar chains could be summarized as follows. 1) The sugar chains of both samples are composed of core 1, Gal beta 1----3GalNAc, and core 2, GlcNAc beta 1----6(Gal beta 1----3)GalNAc. 2) One or two N-acetyllactosamine repeating units extend from the core through GlcNAc beta 1----6Gal and GlcNAc beta 1----3 Gal linkages. 3) Blood group determinants are expressed in accord with the blood types of the donors: sample 1 from a donor of blood type O, Lea+b- contains oligosaccharides with Lea and X determinants, and sample 2 from a donor of B, Lea-b- contains those with H, X, Y, and B determinants.lld:pubmed
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pubmed-article:1904864pubmed:pagination11461-77lld:pubmed
pubmed-article:1904864pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1904864pubmed:articleTitleStructures of mucin-type sugar chains of the galactosyltransferase purified from human milk. Occurrence of the ABO and Lewis blood group determinants.lld:pubmed
pubmed-article:1904864pubmed:affiliationDepartment of Biochemistry, University of Tokyo, Japan.lld:pubmed
pubmed-article:1904864pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1904864pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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