Resolution of DL-tryptophan by affinity chromatography on bovine-serum albumin-agarose columns.

Bovine-serum albumin, known to have antipodal specificity in the binding of tryptophan, was selected as the affinity chromatographic matrix for the attempted chromatographic resolution of DL-tryptophan. Complete resolution was accomplished when Dl-tryptophan was chromatographed on bovine-serum albuminsuccinoylaminoethyl-Sepharose.

Morphology and development of bovine ephemeral fever virus.

The development of the virus of bovine ephemeral fever in mouse brain has been studied by electron microscopy. The virus particles are bullet-shaped, 70 by 145 nm, and slightly tapered toward the rounded end. The outer envelope is closely apposed to an electron-dense shell, about 12 nm thick, but no other internal structure is visible.