Galactosyltransferase and concanavalin A agglutination of cells

D. K. Podolsky, M. M. Weiser, J. T. La Mont, K. J. Isselbacher

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

A correlation has been observed between concanavalin A agglutination of various cell types and the presence of surface membrane galactosyltransferase activity. Moreover, a reduction to less than 50% of cell surface galactosyltransferase activity occurred after treatment with concanavalin A; other cell surface glycosyltransferase enzyme activities examined were unaffected by concanavalin A treatment. To confirm the participation of cell surface galactosyltransferase in concanavalin A induced cell agglutination, the enzyme from rabbit erythrocytes was solubilized by sonication and purified by preparative polyacrylamide gel electrophoresis. It was possible to achieve a purified preparation of rabbit erythrocyte galactosyltransferase by separation on concanavalin A Sepharose. The purified enzyme showed visible immunoprecipitation (Ouchterlony) with concanavalin A. Furthermore, human erythrocytes, which are not normally agglutinated by concanavalin A, became agglutinable by the lectin when the erythrocytes were preincubated with purified galactosyltransferase. These experiments suggest a direct and possible specific role of cell surface galactosyltransferase enzyme in the mechanism of concanavalin A agglutination of cells.

Original languageEnglish (US)
Pages (from-to)904-908
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume71
Issue number3
StatePublished - 1974

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Galactosyltransferases
Agglutination
Concanavalin A
Erythrocytes
Enzymes
Rabbits
Glycosyltransferases
Sonication
Immunoprecipitation
Lectins
Polyacrylamide Gel Electrophoresis
Membranes

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Galactosyltransferase and concanavalin A agglutination of cells. / Podolsky, D. K.; Weiser, M. M.; La Mont, J. T.; Isselbacher, K. J.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 71, No. 3, 1974, p. 904-908.

Research output: Contribution to journalArticle

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AU - Weiser, M. M.

AU - La Mont, J. T.

AU - Isselbacher, K. J.

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N2 - A correlation has been observed between concanavalin A agglutination of various cell types and the presence of surface membrane galactosyltransferase activity. Moreover, a reduction to less than 50% of cell surface galactosyltransferase activity occurred after treatment with concanavalin A; other cell surface glycosyltransferase enzyme activities examined were unaffected by concanavalin A treatment. To confirm the participation of cell surface galactosyltransferase in concanavalin A induced cell agglutination, the enzyme from rabbit erythrocytes was solubilized by sonication and purified by preparative polyacrylamide gel electrophoresis. It was possible to achieve a purified preparation of rabbit erythrocyte galactosyltransferase by separation on concanavalin A Sepharose. The purified enzyme showed visible immunoprecipitation (Ouchterlony) with concanavalin A. Furthermore, human erythrocytes, which are not normally agglutinated by concanavalin A, became agglutinable by the lectin when the erythrocytes were preincubated with purified galactosyltransferase. These experiments suggest a direct and possible specific role of cell surface galactosyltransferase enzyme in the mechanism of concanavalin A agglutination of cells.

AB - A correlation has been observed between concanavalin A agglutination of various cell types and the presence of surface membrane galactosyltransferase activity. Moreover, a reduction to less than 50% of cell surface galactosyltransferase activity occurred after treatment with concanavalin A; other cell surface glycosyltransferase enzyme activities examined were unaffected by concanavalin A treatment. To confirm the participation of cell surface galactosyltransferase in concanavalin A induced cell agglutination, the enzyme from rabbit erythrocytes was solubilized by sonication and purified by preparative polyacrylamide gel electrophoresis. It was possible to achieve a purified preparation of rabbit erythrocyte galactosyltransferase by separation on concanavalin A Sepharose. The purified enzyme showed visible immunoprecipitation (Ouchterlony) with concanavalin A. Furthermore, human erythrocytes, which are not normally agglutinated by concanavalin A, became agglutinable by the lectin when the erythrocytes were preincubated with purified galactosyltransferase. These experiments suggest a direct and possible specific role of cell surface galactosyltransferase enzyme in the mechanism of concanavalin A agglutination of cells.

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