Rapid purification of squirrel monkey retrovirus-H major gag protein by high performance liquid chromatography.
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.
Ikeda
S
S
Department of Biochemistry, Cancer Institute, Okayama University Medical School, Japan.
Tsutsui
K
K
Hatsushika
M
M
Watanabe
S
S
Oda
T
T
D000818:Animals; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D002852:Chromatography, Ion Exchange; D015683:Gene Products, gag; D008970:Molecular Weight; D012190:Retroviridae / Q000032:analysis*; D012191:Retroviridae Proteins / Q000302:isolation & purification*; D012453:Saimiri; D014771:Virion / Q000032:analysis
D015683:Gene Products, gag; D012191:Retroviridae Proteins