Rapid purification of squirrel monkey retrovirus-H major gag protein by high performance liquid chromatography.
Bibliography Type
Author
Ikeda S, Tsutsui K, Hatsushika M, Watanabe S, Oda T.
Summary
The major gag protein (p34) of squirrel monkey retrovirus-H was purified in one chromatographic step by anion-exchange high performance liquid chromatography. The virus in a crude fraction was disrupted with Brij 35 in the presence of three kinds of protease inhibitors. The soluble virus lysate was injected into a Polyanion SI column, and p34 was eluted with a linear salt gradient. The recovery of the protein was about 60%. The purified p34 was nearly homogenous as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and silver staining.