In situ Degradation of the Protein Chain of Potato Virus X at the N- and C-termini

Abstract
The amino acid composition, behavior in SDS[sodium dodecyl sulfate]-polyacrylamide gel electrophoresis and electrophoretic patterns of CNBr peptides were studied for the protein subunits of different preparations of potato virus X (PVX). The protein subunits of PVX can be partially degraded in the intact virus at the N[amino]-terminus by reducing agent-dependent proteases in crude plant sap and by trypsin [EC 3.4.4.4], and at the C[carboxyl]-terminus by reducing agent-independent proteases occurring in some virus preparations.

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