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Volume 271, Number 44, Issue of November 1, 1996 pp. 27810-27817
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Purification and cDNA Cloning of Porcine Brain GDP-L-Fuc:N-Acetyl-beta -D-Glucosaminide alpha 1right-arrow 6Fucosyltransferase

(Received for publication, June 12, 1996, and in revised form, August 6, 1996)

Naofumi Uozumi Dagger , Shusaku Yanagidani Dagger , Eiji Miyoshi Dagger , Yoshito Ihara Dagger , Takahiko Sakuma Dagger , Cong-Xiao Gao Dagger , Tadashi Teshima § , Shigeru Fujii , Tetsuo Shiba § and Naoyuki Taniguchi Dagger

From the Dagger  Department of Biochemistry, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565, Japan,  Laboratory of Chemistry, Kansai Medical University, Hirakata, Osaka 573, Japan, and the § Peptide Institute, Protein Research Foundation, 4-1-2 Ina, Minoh, Osaka 562, Japan

GDP-L-Fuc:N-acetyl-beta -D-glucosaminide alpha 1right-arrow6fucosyltransferase (alpha 1-6FucT; EC 2.4.1.68), which catalyzes the transfer of fucose from GDP-Fuc to N-linked type complex glycopeptides, was purified from a Triton X-100 extract of porcine brain microsomes. The purification procedures included sequential affinity chromatographies on GlcNAcbeta 1-2Manalpha 1-6(GlcNAcbeta 1-2Manalpha 1-2)Manbeta 1-4GlcNAcbeta 1-4GlcNAc-Asn-Sepharose 4B and synthetic GDP-hexanolamine-Sepharose 4B columns. The enzyme was recovered in a 12% final yield with a 440,000-fold increase in specific activity. SDS-polyacrylamide gel electrophoresis of the purified enzyme gave a major band corresponding to an apparent molecular mass of 58 kDa. The alpha 1-6FucT has 575 amino acids and no putative N-glycosylation sites. The cDNA was cloned in to pSVK3 and was then transiently transfected into COS-1 cells. alpha 1-6FucT activity was found to be high in the transfected cells, as compared with non- or mock-transfected cells. Northern blotting analyses of rat adult tissues showed that alpha 1-6FucT was highly expressed in brain. No sequence homology was found with other previously cloned fucosyltransferases, but the enzyme appears to be a type II transmembrane protein like the other glycosyltransferases.


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