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  • Title: Isolation, characterization, and expression of a cDNA encoding N-acetylglucosaminyltransferase V.
    Author: Shoreibah M, Perng GS, Adler B, Weinstein J, Basu R, Cupples R, Wen D, Browne JK, Buckhaults P, Fregien N, Pierce M.
    Journal: J Biol Chem; 1993 Jul 25; 268(21):15381-5. PubMed ID: 8340368.
    Abstract:
    A cDNA clone for the complete coding sequence for alpha-1,3(6)-mannosylglycoprotein beta-1,6-N-acetylglucosaminyltransferase V (GlcNAc-T V, EC 2.4.1.155) was isolated and expressed in COS-7 cells. Degenerate oligonucleotide primers for polymerase chain reaction were synthesized based on the amino acid sequence of three tryptic peptides isolated from affinity-purified GlcNAc-T V. Polymerase chain reaction amplimers were isolated from rat and mouse mRNA. A cDNA-encoding full-length enzyme was isolated from a rat 1 cell (EJ-ras-transformed) library and sequenced. Transient expression of this clone in COS-7 cells, followed by enzymatic activity assays, demonstrated that this cDNA sequence encodes GlcNAc-T V. Northern analysis of rat kidney mRNA revealed a single band corresponding to a length of about 7 kilobases. Sequence analysis of the cDNA clone demonstrated an open reading frame that encoded a type II membrane protein of 740 amino acids.
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