Literature DB >> 2956949

Activity of UDP-GlcNAc:alpha-mannoside beta(1,6)N-acetylglucosaminyltransferase (GnT V) in cultured cells using a synthetic trisaccharide acceptor.

M Pierce, J Arango, S H Tahir, O Hindsgaul.   

Abstract

N-acetylglucosaminyltransferase V activity has been measured under saturating conditions in the extracts of seven cultured cell lines using as substrates, UDP-[3H]-GlcNAc and a synthetic 8-methoxylcarbonyloctyl trisaccharide. The unreacted sugar-nucleotide and its breakdown products were separated from the radiolabeled tetrasaccharide product by reverse-phase chromatography. Enzyme activity was present in six of the cell lines, which were derived originally from either human, mouse, or hamster tissues, with the highest activity in mouse lymphoma BW5147 cells. The PHAR 2.1 variant cell line, derived from the BW5147 line, expressed no detectable activity.

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Year:  1987        PMID： 2956949     DOI： 10.1016/0006-291x(87)90582-1

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  5 in total

1.  NMR structural characterization of substrates bound to N-acetylglucosaminyltransferase V.

Authors:  Megan A Macnaughtan; Maria Kamar; Gerardo Alvarez-Manilla; Andre Venot; John Glushka; J Michael Pierce; James H Prestegard
Journal:  J Mol Biol       Date:  2006-12-12       Impact factor: 5.469

2.  Preparation of antisera to recombinant, soluble N-acetylglucosaminyltransferase V and its visualization in situ.

Authors:  L Chen; N Zhang; B Adler; J Browne; N Freigen; M Pierce
Journal:  Glycoconj J       Date:  1995-12       Impact factor: 2.916

3.  Incomplete synthesis of N-glycans in congenital dyserythropoietic anemia type II caused by a defect in the gene encoding alpha-mannosidase II.

Authors:  M N Fukuda; K A Masri; A Dell; L Luzzatto; K W Moremen
Journal:  Proc Natl Acad Sci U S A       Date:  1990-10       Impact factor: 11.205

4.  Control of carbohydrate processing: increased beta-1,6 branching in N-linked carbohydrates of Lec9 CHO mutants appears to arise from a defect in oligosaccharide-dolichol biosynthesis.

Authors:  A G Rosenwald; P Stanley; S S Krag
Journal:  Mol Cell Biol       Date:  1989-03       Impact factor: 4.272

5.  The Lec4A CHO glycosylation mutant arises from miscompartmentalization of a Golgi glycosyltransferase.

Authors:  W Chaney; S Sundaram; N Friedman; P Stanley
Journal:  J Cell Biol       Date:  1989-11       Impact factor: 10.539
  5 in total

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