Elektrophoretische Untersuchungen der Α-Proteine dreier Tabakmosaikvirus-Stämme

摘要: In the present paper we studied relations between mobility of RNA-free proteins three strains tobacco mosaic virus and pH. The were prepared by alcaline degradation native virus. We used a carefully purified product for electrophoretic measurements, so-called Α-protein (sedimentation constant 4,6 S; molecular weight about 90 000). verified sedimentation measurements electron microscopy that this protein within pH-range 2,5 - 6,0 ist reaggregated into rods. these rods is identical with respective (fig. 1). Below pH above differs greatly from 1 2). To explain results it presumed, determined only those acid basic groups which are situated on or near surface migrating particle. Since in case RNA would be unable to influence particles, complete rod-like aggregates becomes understandable. changes at thus explained non homogeneous distribution principally groups. According assumption mainly inside not