Thermal solubility of gene 8 coat protein in 2 M urea from fd phage

Chun, Paul W.; Herschleb, William P.; Buckley, R.; Bliziotes, Michael; Son, U. T.; Krista, Mary L.

doi:10.1016/s0006-291x(74)80274-3

Cited by 2 publications

(1 citation statement)

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“…Attempts to prepare milligram amounts of the adsorption protein in highly purified form have been hampered by a number of problems. One of the difficulties is that the coat proteins are soluble only in detergents or under denaturing conditions (Knippers and Hoffmann-Berling, 1966;Chun et al, 1974;Marco, 1975). This property restricts the type of purification procedures that can be used for the isolation of the adsorption protein.…”

Section: Resultsmentioning

confidence: 99%

Adsorption protein of the bacteriophage fd: isolation, molecular properties, and location in the virus

Goldsmith¹,

Konigsberg²

1977

Biochemistry

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The adsorption (minor coat) protein of the bacteriophage fd has been implicated to function in several steps of viral morphogenesis. The protein has been purified by sodium dodecyl sulfate gel filtration after dissociation of the virus. The adsorption protein preparation was estimated to have less than 5% contamination by analysis on sodium dodecyl sulfate-polyacrylamide gels and by the results of semiquantitative dansyl-Edman degradation. The amino-terminal sequence of the adsorption protein is H2N-Ala-Glx-Thr-Val-Glx-Ser-Pro-Leu-Pro-. Carboxypeptidase A plus B digestion of the protein under a variety of denaturing conditions did not release any amino acids. There are 3-4 adsorption proteins per virion as estimated by the distribution of E114C]leucine between the major and minor coat protein peaks on sodium dodecyl sulfate-polyacrylamide gels. Adsorption protein-specific antibodies were induced in the rabbit and used as electronmicroscopic markers to determine the position of the adsorption proteins in the viral particle. The adsorption proteins were found at only one end of the filamentous viral particles.

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Section: Resultsmentioning

confidence: 99%