By Paul Hyman, Timothy Harrah
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Extra info for Bacteriophage T4 tail fibers as a basis for structured assemblies
Comparison of phage inactivation when Mab is pre-treated (or not) with an oligopeptide identical to the epitope insert. two strains. This supported the hypothesis that the inserted Mab epitope was functional in the tail fiber and accessible to molecules outside of the tail fiber. We further showed that the extent of phage inactivation was a function of how long the phage and Mab were allowed to interact (with the secondary antiserum incubation time held constant) (Figure 4-5A) and that the extent of inactivation was correlated with the amount of Mab used (again with constant secondary antiserum) (Figure 4-5B).
4. Tail fiber modifications We and others working in the Goldberg lab have succeeded in identifying or introducing a number of changes into tail fiber proteins. These changes include deletions and insertions, and epitopes or other peptides as attachment sites for other molecules. For the following sections all bacteria and phage strains are listed in Appendix F, growth media and other buffers are described in Appendix G and general stock preparation and mutant generation methods are described in Appendix H.
Cysep 329 is a proprietary water soluble cationic polyquaternary amine that 18 Bacteriophage Tail Fibers selectively precipitates P23* and other remaining contaminant proteins, leaving the LTF in solution. Maximum efficiency was achieved in the absence of sodium chloride, and therefore the buffer was exchanged prior to flocculation. Similar results were obtained using Bio-Rad AG 1-X4 quaternary amine functionalized chromatography resin. Following centrifugation, excess Cysep was removed and the purified protein was concentrated.
Bacteriophage T4 tail fibers as a basis for structured assemblies by Paul Hyman, Timothy Harrah