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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
21
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pubmed:dateCreated |
1993-8-30
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pubmed:databankReference | |
pubmed: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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15381-5
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pubmed:dateRevised |
2008-8-5
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pubmed:meshHeading |
pubmed-meshheading:8340368-Amino Acid Sequence,
pubmed-meshheading:8340368-Animals,
pubmed-meshheading:8340368-Base Sequence,
pubmed-meshheading:8340368-Cell Line,
pubmed-meshheading:8340368-DNA,
pubmed-meshheading:8340368-Kidney,
pubmed-meshheading:8340368-Mice,
pubmed-meshheading:8340368-Molecular Sequence Data,
pubmed-meshheading:8340368-N-Acetylglucosaminyltransferases,
pubmed-meshheading:8340368-Polymerase Chain Reaction,
pubmed-meshheading:8340368-RNA, Messenger,
pubmed-meshheading:8340368-Rats
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pubmed:year |
1993
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pubmed:articleTitle |
Isolation, characterization, and expression of a cDNA encoding N-acetylglucosaminyltransferase V.
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pubmed:affiliation |
Department of Biochemistry, University of Georgia, Athens 30602.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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