Chromatographic behavior of pea lectin receptors from the 6C3HED murine ascites tumor.

We have previously shown that pea lectin and concanavalin A bind to different receptors as well as to common receptors on the cell surface of 6C3HED murine ascites tumor cells (Allen, H.J. nd Johnson, E.A.Z. (1976) Biochim. Biophys. Acta 436, 557-566). We have characterized the metabolically labeled pea lectin receptor from trypsinates of viable tumor cells by gel filtration and affinity chromatography. The pea lectin receptor eluted as an apparent high molecular weight glycopeptice (Mr 200 000) from Sephadex G-200 columns. Other glycopeptides were present in the trypsinates but they did not bind to either concanavalin A or to pea lectin in significant amounts. The high molecular weight glycopeptide was resistant to digestion by a high concentration of trypsin but it was absent in non-specific protease digests of viable cells. Sequential lectin affinity chromatography of Nonidet P-40 extracts of cells permitted the probable identification of the native glycoprotein corresponding to the high molecular weight glycopeptide which binds to pea lectin.