Abstract
An antiviral factor from virus-infected plants (AVF) was purified in an active form on SDS-polyacrylamide gels. AVF binds to concanavalin A and is partially sensitive to α-glucosidase. It is sensitive to pronase only when incubated in conditions suitable for proteolysis of glycoproteins. Alkaline phosphatase affected the electrophoretic mobility of AVF, but did not abolish antiviral activity. AVF was insensitive to DNase, -glucosidase and pancreatic lipase. The AVF band obtained upon electrophoresis could be stained with Coomassie blue and by the Schiff-periodate procedure for carbohydrates. AVF is considered to be a phosphoglycoprotein with a mol. wt. of about 22000.