Studies on phytohemagglutinins: XXII. Isolation and characterization of a lymphocyte receptor for concanavalin A |
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Authors: | Jarmila Pospí?ilova C Ha?kovec G Entlicher J Kocourek |
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Institution: | 1. Department of Biochemistry, Charles University, Albertov 2030, 128 40 Prague 2 Czechoslovakia;2. Institute of Experimental Biology and Genetics, Czechoslovak Academy of Sciences, Budějovická 1083, 142 20 Prague 4-Kr?. Czechoslovakia |
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Abstract: | A receptor glycopeptide for concanavalin A was isolated from calf thymocytes by a method originally devised for the isolation of a lectin receptor from human erythrocytes (Kubánek, J., Entlicher, G.; and Kocourek, J. 1973] Biochim, Biophys. Acta 304, 93–102). The method consisted of pronase digestion of the lipid-depleted thymocyte membrane material followed by ethanol fractionation, separation on Sephadex and preparative paper electrophoresis. The isolated glycopeptide contains 10.4% of neutral sugar. The molar ratios of the sugar components mannose, galactose, glucosamine, glucose, fucose and sialic acid are 3 : 2 : 2 : 1 : 1 : 1. The minimum molecular weight calculated from the sugar composition is about 12 000.Concanavalin A receptor activity of the glycopeptide was demonstrated in three different ways: (i) Reduction of the 125I-labeled concanavalin A binding to thymocytes. (ii) Prevention of concanavalin A induced agglutination of calf thymocytes. (iii) Inhibition of concanavalin A stimulated DNA synthesis in calf and rabbit thymocytes and rabbit lymph node lymphocytes cultivated in vitro.The isolated glycopeptide seems to be involved in the interaction of lymphocytes with concanavalin A and the subsequent stimulation. |
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