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Titolo:
CDNA CLONING AND EXPRESSION OF BOVINE UDP-N-ACETYLGLUCOSAMINE - ALPHA-1,3-D-MANNOSIDE BETA-1,4-N-ACETYLGLUCOSAMINYLTRANSFERASE IV
Autore:
MINOWA MT; OGURI S; YOSHIDA A; HARA T; IWAMATSU A; IKENAGA H; TAKEUCHI M;
Indirizzi:
KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL,KANAZAWA KU,1-13-5 FUKU URA YOKOHAMA KANAGAWA 236000 JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL,KANAZAWA KU YOKOHAMA KANAGAWA 236000 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 19, volume: 273, anno: 1998,
pagine: 11556 - 11562
SICI:
0021-9258(1998)273:19<11556:CCAEOB>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALPHA-3-D-MANNOSIDE BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE-I GENE; GLYCOPROTEIN-SYNTHESIS; MOLECULAR-CLONING; GOLGI RETENTION; UDP-N-ACETYLGLUCOSAMINE-ALPHA-3-D-MANNOSIDE BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFE; ALPHA-1-ACID GLYCOPROTEIN; HUMAN ERYTHROPOIETIN; SUGAR CHAINS; RAT-KIDNEY; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
M.T. Minowa et al., "CDNA CLONING AND EXPRESSION OF BOVINE UDP-N-ACETYLGLUCOSAMINE - ALPHA-1,3-D-MANNOSIDE BETA-1,4-N-ACETYLGLUCOSAMINYLTRANSFERASE IV", The Journal of biological chemistry, 273(19), 1998, pp. 11556-11562

Abstract

UDP-N-acetulglucosamine:alpha 1,3-D-mannoside beta 1,4-N-acetylglucosaminyltransferase (GnT-IV) is one of the essential enzymes in the production of tri-and tetra-antennary Asn-linked sugar chains. Recently, we have successfully purified GnT-IV from bovine small intestine. Basedon the partial amino acid sequence of the purified bovine GnT-IV enzyme, its cDNA has been cloned from bovine small intestine. The open reading frame is 1,605 base pairs long, and this sequence produced GnT-IVactivity on transient expression in COS-7 cells. Although the deducedamino acid sequence does not have any significant homology with otherknown N-acetylglucosaminyltransferases (GnTs), the hydrophobicity profile showed a typical type II transmembrane protein structure, which is common to many glycosyltransferases, N-terminal amino acid sequencing of the purified GnT-IV revealed that 92 amino acids, including a transmembrane region, were truncated during purification. Of the three potential N-glycosylation sites Asn-458 was actually glycosylated in thepurified enzyme, although this N-glycosylation site could be abolished without any reduction in GnT-IV activity. Serial deletions at both the N and C termini proved that the catalytic domain of GnT-IV is located in the central region of the enzyme. The GnT-IV mRNA level correlated with enzymatic activity in the various bovine tissues tested.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 03:14:01