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A coat protein from bacteriophage fd: I. Hydrodynamic measurements and biological characterization

MPS-Authors
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Knippers,  R.
Max Planck Institute for Medical Research, Max Planck Society;

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Hoffman-Berling,  Hartmut
Max Planck Institute for Medical Research, Max Planck Society;

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http://www.sciencedirect.com/science/article/pii/0022283666900994/pdf?md5=b3ad61f826bec88e17077894ef15c672&pid=1-s2.0-0022283666900994-main.pdf
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https://doi.org/10.1016/0022-2836(66)90099-4
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Citation

Knippers, R., & Hoffman-Berling, H. (1966). A coat protein from bacteriophage fd: I. Hydrodynamic measurements and biological characterization. Journal of Molecular Biology (London), 21(2), 281-292. doi:10.1016/0022-2836(66)90099-4.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-5222-C
Abstract
A coat protein has been isolated from highly purified fd bacteriophage disintegrated in phenol. Dissociation of the isolated protein to the monomeric state has only been achieved in 1% sodium dodecyl sulphate. At lower concentrations of the detergent as well as in several other solvents, the protein exists in the form of uniformly sized oligomers, probably heptamers or octamers. Protein dissolved in concentrated urea and dialysed versus neutral buffer aggregates to give rod-shaped particles with approximately the diameter of virus particles, but otherwise unlike virus in appearance. Such protein functions in blocking fd receptive sites of the bacterial host and in inactivating fd antiserum, although without complete exhaustion. The implications of these findings for the structure of the aggregated protein are discussed.