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The amino acid composition, behaviour in SDS-polyacrylamide gel electrophoresis and electrophoretic patterns of cyanogen bromide peptides were studied for the protein subunits of different preparations of potato virus X (PVX). The results indicate that the protein subunits of PVX can be partially degraded in the intact virus at the N-terminus by reducing agent-dependent proteases in crude plant sap and by trypsin, and at the C-terminus by reducing agent-independent proteases occurring in some virus preparations.
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