Summary
This paper reports the isolation and biochemical characterization of a major concanavalin A (Con A)-binding cell surface protein (protein 2, Mr 75–85 kD) from normal and chronic myeloid leukemic (CML) granulocytes. Our studies show that protein 2 has two differentially glycosylated forms, protein 2 a (Mr 75–85 kD), which does not bind the lectin RCA, and protein 2 b (Mr 80–90 kD), which does. Both molecules show identical retention times on reverse-phase HPLC, irrespective of the cell source. By the procedure used the amount of 2 a obtained is about 2.4 times more than that of 2 b in normal cells and about 2.6 times more in CML cells. Furthermore, both are ∼ 2.4-fold more in CML granulocytes. A polyclonal antibody to protein 2 a also immunostains protein 2b. The antibody to protein 2 a does not prevent Con A binding but inhibits its internalization. Similarity of the molecules from both the cell types and their increased amounts in CML granulocytes suggest that factors/components other than its structure and amount are responsible for the known defective internalization of Con A by CML granulocytes.
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Hingorani, R., Zingde, S.M., Tankkar, A. et al. A major concanavalin-A-binding cell surface protein from normal and leukemic granulocytes: Isolation and characterization. Ann Hematol 65, 175–183 (1992). https://doi.org/10.1007/BF01703111
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DOI: https://doi.org/10.1007/BF01703111