Stream Double Refraction of Virus Proteins

Double refraction of flow was observed as early as 1874 byMaxwell (see Ambronn and Frey (1)) who showed that Canada balsam becomes optically anisotropic when it is stirred vigorously.Some years later Kundt found that gelatin sols show this phenomenon (1).Freundlich (7) observed that sols of vanadium pentoxide and of certain dyes show stream double refraction.He further pointed out that the particles of the vanadium pentoxide sols are rod-shaped, and concluded that the double refraction was due to the orientation of the rod-shaped particles in the viscous stream.More recently, von Muralt and Edsall ( 13) have shown that myosin, the globulin of muscle, shows the phenomenon to a marked extent.Ovoglobulin and egg albumin gel, the latter at high pH values, have been reported by Boehm and Signer (5) to show stream double refraction.Takahashi and Rawlins (19) have reported that the juice expressed from tobacco plants infected with tobacco mosaic virus exhibited this property, and more recently they have shown that purified tobacco mosaic virus protein behaves similarly.Finally, other plant virus proteins, those of aucuba mosaic of tomato, enation mosaic of tomato, and Ainsworth's cucumber mosaics Nos. 3 and 4, have been shown by Bawden and Pirie (2) to exhibit double refraction of flow.These workers regard all of these viruses as being related to that of tobacco mosaic.Because of Freundlich's findings, Takahashi and Rawlins regarded the double refraction of flow in tobacco mosaic virus solutions as being due to the orientation of asymmetrical particles, and, by a method which will be mentioned later, limited this to the orientation of rod-shaped particles.