| First Author | Shoreibah M | Year | 1993 |
| Journal | J Biol Chem | Volume | 268 |
| Issue | 21 | Pages | 15381-5 |
| PubMed ID | 8340368 | Mgi Jnum | J:41554 |
| Mgi Id | MGI:894032 | Doi | 10.1016/s0021-9258(18)82268-2 |
| Citation | Shoreibah M, et al. (1993) Isolation, characterization, and expression of a cDNA encoding N-acetylglucosaminyltransferase V. J Biol Chem 268(21):15381-5 |
| abstractText | 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. |
