This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Yamashita, K. Articles by Kobata, A. Search for Related Content PubMed PubMed Citation Articles by Yamashita, K. Articles by Kobata, A.

Comparative Study of the Sugar Chains of -Glutamyltranspeptidases Purified from Rat Liver and Rat AH-66 Hepatoma Cells¹

Department of Biochemistry, Kobe University School of Medicine, Chuo-ku, Kobe, Japan [K. Y., A. H., A. K.], and Biochemistry Laboratory, Cancer Institute [N. T., N. Y.], and Department of Biochemistry [Y. T.], Hokkaido University School of Medicine, Sapporo, Japan

A comparative study using hydrazinolysis has revealed that the oligosaccharide pattern of -glutamyltranspeptidase purified from rat AH-66 hepatoma cells is very different from that of the enzyme from rat liver. Studies of oligosaccharides in each fraction have clarified the structural basis of the difference found in the sugar chains of the two enzymes. The sugar chains of the liver enzyme were all acidic, while 28% of those of the hepatoma enzyme were neutral, the latter being composed of high-mannose-type and complex-type sugar chains. Three prominent structural differences were found in the acidic sugar chains of the two enzymes: (a) the sugar chains of the liver enzyme have complete outer chains, Galß14GlcNAcß1, while many of those of the hepatoma enzyme have incomplete outer chains without galactose (Gal); (b) the Galß14GlcNAcß1Galß14GlcNAcß1 group is found in the sugar chains of the liver enzyme but not in those of the hepatoma enzyme; (c) more than 40% of the sugar chains of the hepatoma enzyme contain bisect N-acetylglucosamine (GlcNAc) residue which is not found in those of the liver enzyme.

Furthermore, the total number of asparagine-linked sugar chains in one molecule of hepatoma enzyme was about 4 times that found in one molecule of liver enzyme.

¹ This work was supported by Grant-in-Aid for Cancer Research, the Ministry of Education, Science and Culture of Japan, and by a research grant from Yamanouchi Foundation for Research on Metabolic Disorders.

² To whom requests for reprints should be addressed, at the Department of Biochemistry, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108, Japan.

Received 1/24/83. Accepted 8/ 2/83.

This article has been cited by other articles:

				S.-K. Kang, T.-W. Chung, J.-Y. Lee, Y.-C. Lee, R. E. Morton, and C.-H. Kim The Hepatitis B Virus X Protein Inhibits Secretion of Apolipoprotein B by Enhancing the Expression of N-Acetylglucosaminyltransferase III J. Biol. Chem., July 2, 2004; 279(27): 28106 - 28112. [Abstract] [Full Text] [PDF]

				H. Ueda, H. Matsumoto, N. Takahashi, and H. Ogawa Psathyrella velutina Mushroom Lectin Exhibits High Affinity toward Sialoglycoproteins Possessing Terminal N-Acetylneuraminic Acid alpha 2,3-Linked to Penultimate Galactose Residues of Trisialyl N-Glycans. COMPARISON WITH OTHER SIALIC ACID-SPECIFIC LECTINS J. Biol. Chem., July 5, 2002; 277(28): 24916 - 24925. [Abstract] [Full Text] [PDF]