Shevchenko N A, Boĭkov P Ia, Lichina M V, Kononova S D, Gumanov L L
Biokhimiia. 1976 Jan;41(1):3-13.
A method of preparative isolation of membrane rIIB protein from bacteriophage T4 is worked out. Conditions are found to maximal rIIB protein accumulation in membranes of E. coli cells infected with bacteriophage T4. The membrane isolation by ultracentrifugation is substituted with their sedimentation from polyethyleneglycol solutions by low-speed centrifugation. A fraction, enriched with rIIB protein, is obtained using the treatment of cell walls with detergents. Preparative polyacrylamide gel electrophoresis in the presence of sodium dodecylsulphate was used for further rIIB protein purification. The method described can be applied for the purification and preparative isolation of memorane and poor-soluble proteins. The problem on location and ufunctioning of rIIB protein is discussed.
