JBC Ideal method for primary cell transfection

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Minowa, M. T.
Right arrow Articles by Takeuchi, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Minowa, M. T.
Right arrow Articles by Takeuchi, M.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 273, Issue 19, 11556-11562, May 8, 1998

cDNA Cloning and Expression of Bovine UDP-N-Acetylglucosamine:alpha 1,3-D-Mannoside beta 1,4-N-Acetylglucosaminyltransferase IV

Mari Toba Minowa, Suguru Oguri, Aruto Yoshida, Tomoka Hara, Akihiro Iwamatsu, Hiroshi Ikenaga, and Makoto Takeuchi

From the Central Laboratories for Key Technology, KIRIN Brewery Co., Ltd., 1-13-5 Fuku-ura, Kanazawa-ku, Yokohama, 236-0004, Japan

UDP-N-acetylglucosamine: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. Based on 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-IV activity on transient expression in COS-7 cells. Although the deduced amino acid sequence does not have any significant homology with other known 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 the purified 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.


Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
GlycobiologyHome page
S. Uemura, T. Kurose, T. Suzuki, S. Yoshida, M. Ito, M. Saito, M. Horiuchi, F. Inagaki, Y. Igarashi, and J.-i. Inokuchi
Substitution of the N-glycan function in glycosyltransferases by specific amino acids: ST3Gal-V as a model enzyme
Glycobiology, March 1, 2006; 16(3): 258 - 270.
[Abstract] [Full Text] [PDF]


Home page
GlycobiologyHome page
A. Kobata
The history of glycobiology in Japan
Glycobiology, August 1, 2001; 11(8): 99R - 105R.
[Abstract] [Full Text] [PDF]


Home page
GlycobiologyHome page
L. L. Christensen, U. B. Jensen, P. Bross, and T. F. Orntoft
The C-terminal N-glycosylation sites of the human {alpha}1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V and -VI) are necessary for the expression of full enzyme activity
Glycobiology, September 1, 2000; 10(9): 931 - 939.
[Abstract] [Full Text] [PDF]


Home page
GlycobiologyHome page
K. Fukuta, R. Abe, T. Yokomatsu, N. Kono, M. Asanagi, F. Omae, M. T. Minowa, M. Takeuchi, and T. Makino
Remodeling of sugar chain structures of human interferon-{gamma}
Glycobiology, April 1, 2000; 10(4): 421 - 430.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
J. Nakayama, J.-C. Yeh, A. K. Misra, S. Ito, T. Katsuyama, and M. Fukuda
Expression cloning of a human alpha 1,4-N-acetylglucosaminyltransferase that forms GlcNAcalpha 1right-arrow4Galbeta right-arrowR, a glycan specifically expressed in the gastric gland mucous cell-type mucin
PNAS, August 3, 1999; 96(16): 8991 - 8996.
[Abstract] [Full Text] [PDF]


Home page
Cancer Res.Home page
S. Takamatsu, S. Oguri, M. T. Minowa, A. Yoshida, K. Nakamura, M. Takeuchi, and A. Kobata
Unusually High Expression of N-Acetylglucosaminyltransferase-IVa in Human Choriocarcinoma Cell Lines: A Possible Enzymatic Basis of the Formation of Abnormal Biantennary Sugar Chain
Cancer Res., August 1, 1999; 59(16): 3949 - 3953.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Taguchi, T. Ogawa, S. Inoue, Y. Inoue, Y. Sakamoto, H. Korekane, and N. Taniguchi
Purification and Characterization of UDP-GlcNAc: GlcNAcbeta 1-6(GlcNAcbeta 1-2)Manalpha 1-R [GlcNAc to Man]-beta 1, 4-N-acetylglucosaminyltransferase VI from Hen Oviduct
J. Biol. Chem., October 13, 2000; 275(42): 32598 - 32602.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Y. Sakamoto, T. Taguchi, K. Honke, H. Korekane, H. Watanabe, Y. Tano, N. Dohmae, K. Takio, A. Horii, and N. Taniguchi
Molecular Cloning and Expression of cDNA Encoding Chicken UDP-N-acetyl-D-glucosamine (GlcNAc): GlcNAcbeta 1-6(GlcNAcbeta 1-2)- Manalpha 1-R[GlcNAc to Man]beta 1,4N-acetylglucosaminyltransferase VI
J. Biol. Chem., November 10, 2000; 275(46): 36029 - 36034.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.