J. Biochem, 1995, Vol. 118, No. 3 541-545
© 1995 Japanese Biochemical Society
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Purification and Characterization of Secretory-Type GDP-L-Fucose: ß-D-Galactoside 2-
-L-Fucosyltransferase from Human Gastric Mucosa1
Department of Legal Medicine, Kurume University School of Medicine Kurume, Fukuoka 830
2To whom correspondence should be addressed. Phone: + 81-942-31-7554, Fax: +81-942-31-7700
-(1, 2)-Fucosyltransferase (GDP-L-fucose: ß-D-galactoside 2--L-fucosyltransferase) from human gastric mucosa was purified to homogeneity by column chromatographies on Ultrogel AcA34, phenyl-Sepharose, hydroxylapatite, SP-Sephadex, and GDP-hexanol-amine Sepharose. The molecular weight of the purified enzyme was estimated to be 65, 000 by SDS-PAGE. The Km value of this enzyme for a type 1 sugar acceptor was a little smaller than that for a type 2 one, indicating this enzyme is a secretor-type -(1, 2)-fucosyltrans-ferase. However, the difference between the Km value for a type 1 precursor and that for a type 2 one was very small, suggesting that this enzyme can use both types of precursors as sugar acceptors approximately equally, unlike the purified -(1, 2)-fucosyltransferase from human serum as the secretor-type reported previously. The characteristics of the purified enzyme were compared with those of H-type -(1, 2)-fucosyltransferase from human plasma. The activities of both enzymes were inhibited by salt and N-ethylmaleimide, but they showed a significant difference in their divalent cation requirements.
1This work was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.
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