PMID: 6965465Jan 15, 1980Paper

The major sialoglycoprotein of human T-lymphocytes

Carbohydrate Research
M Saito, T Osawa

Abstract

Human, peripheral-blood T-lymphocytes and human, T-lymphoblastoid cells of a MOLT 4B cell-line were surface-labeled by lactoperoxidase-catalyzed iodination, periodate and sodium borotritide, and galactose oxidase and sodium borotritide, and analyzed by dodecyl sodium sulfate-polyacrylamide gel-electrophoresis. Both types of cells were found to show a major, cell-surface sialoglycoprotein with an apparent mol. wt. of 95,000. After neuraminidase treatment, this glycoprotein showed a higher mol. wt. of 120,000. The major sialoglycoprotein of both types of cells bound to wheat-germ agglutinin and concanavalin A and, after neuraminidase treatment, to Arachis hypogaea agglutinin. The glycopeptides obtained from these glycoproteins by Pronase digestion gave similar elution-profiles on Sephadex G-50 gel filtration. These results suggest that the major sialoglycoprotein of normal T cells and that of MOLT 4B cells are very similar, if not identical.

References

Nov 15, 1977·International Journal of Cancer. Journal International Du Cancer·L C AnderssonH Wigzell
Jul 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·L C AnderssonH Wigzell
Mar 8, 1979·Biochimica Et Biophysica Acta·R H Kramer, E S Canellakis
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