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Carbohydrate Analysis of Immunoglobulin G Myeloma Proteins by Lectin and High Performance Liquid Chromatography: Role of Glycosyltransferases in the Structures¹

Second Department of Internal Medicine, Osaka University Medical School, 1-1-50 Fukushima, Fukushima-ku, Osaka 553 [T. N., Y. K., Y. T., M. I., T. K., H. N., T. Y., S. T.], and Department of Biochemistry, Osaka University Medical School, 4-3-57, Nakanoshima, Kita-ku, Osaka 530 [S. F., A. N., N. T.], Japan

The carbohydrate structures and the enzymatic basis for glycosylation of IgG by bone marrow plasma cells were determined in 7 patients with monoclonal gammopathy of undetermined significance and 22 patients with IgG MM. Lectin-binding analysis showed that in all cases of monoclonal gammopathy of undetermined significance and normal controls the IgG heavy chains bound to Ricinus communis agglutinin more strongly than to concanavalin A. In contrast, the IgG in 11 of the 17 advanced cases of MM (stages II and III) studied reacted to concanavalin A more strongly. Structural analysis showed that the reduced R. communis agglutinin binding capacity of these MM IgGs was due to hypogalactosylation of IgG. The galactosyltransferase and N-acetylglucosaminyltransferase III activities of the bone marrow myeloma cells from 5 MM cases were found to have a low enzyme activity ratio of galactosyltransferase to N-acetylglucosaminyltransferase III which reflects the hypogalactosylation. This indicates that the difference in the carbohydrate moieties observed in myeloma proteins is due to variations in the activities of the two glycosyltransferases.

¹ This work was supported by Grants-in-Aid for Cancer Research and Scientific Research on Priority Areas from the Ministry of Education, Science and Culture, Japan.

² To whom requests for reprints should be addressed.

Received 12/11/89. Revised 4/16/90.

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