Abstract
Summary
The effects of three proteases, trypsin, papain, and pronase, upon the major glycoprotein of horse erythrocyte membranes were examined. By three independent criteria, papain was the most effective. Sodium dodecyl sulfate polyacryla-mide gel electrophoresis of stroma derived from papain-treated erythrocytes revealed the loss of the major glycoprotein band characteristic of this membrane. Concomitant with the loss of the major glycoprotein band, fragments were released from the erythrocyte which had a carbohydrate composition similar to that of the intact glycoprotein. Also, reactivity of the treated erythrocytes with infectious mononucleosis antibody, a property associated with the major glycoprotein, was reduced. Only a portion of the membrane glycoprotein was susceptible to pronase action and none was cleaved by trypsin.
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