Rapid analysis of lambda gt11 fusion proteins without subcloning or lysogen induction.
Current methods of analyzing fusion proteins from lambda gt11 clones involve either subcloning of the insert DNA into a plasmid expression vector or production of lambda gt11 lysogens that are subsequently induced. Both of these methods can be quite time-consuming. The present communication describes a novel strategy for induction of the fusion protein that is both simple and rapid. Liquid cultures of E. coli Y1090R- infected with the lambda gt11 clone were induced directly to produce the fusion protein. Following the preparation of a crude bacterial cell lysate, fusion products were subjected to Western blot analysis.
Runge
S W
SW
Department of Medical Biochemistry, Ohio State University, Columbus 43210.
D000818:Animals; D010582:Bacteriophage lambda / Q000235:genetics*; D015153:Blotting, Western; D003001:Cloning, Molecular / Q000379:methods*; D008242:Lysogeny / Q000235:genetics*; D051381:Rats; D014407:Tumor Cells, Cultured; D014760:Viral Fusion Proteins / Q000032:analysis* / Q000235:genetics
D014760:Viral Fusion Proteins