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Publication : Cloning and sequencing of a full-length cDNA of mouse N-acetylglucosamine (beta 1-4)galactosyltransferase.

First Author  Nakazawa K Year  1988
Journal  J Biochem Volume  104
Issue  2 Pages  165-8
PubMed ID  3141392 Mgi Jnum  J:41033
Mgi Id  MGI:892761 Doi  10.1093/oxfordjournals.jbchem.a122434
Citation  Nakazawa K, et al. (1988) Cloning and sequencing of a full-length cDNA of mouse N-acetylglucosamine (beta 1-4)galactosyltransferase. J Biochem 104(2):165-8
abstractText  A full-length cDNA clone for mouse N-acetylglucosamine (beta 1-4)galactosyltransferase (beta 1-4GT) [EC 2.4.1.90] and several clones diverged from the beta 1-4GT cDNA were isolated from a mouse F9 cDNA library and then sequenced. The beta 1-4GT cDNA has an open reading frame consisting of 399 amino acids. The homology at the amino acid level is 80 and 91% as to the partial sequences of bovine and human milk beta 1-4GT, respectively. The general enzyme structure of the beta 1-4GT seems to be similar to that of a rat beta-galactoside (alpha 2-6) sialyltransferase. Junctions of the common and divergent regions of cDNA have dinucleotides, AG, suggesting that the variety of cDNA clones is generated through alternative splicing.
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