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. 1974 Sep;14(3):503–508. doi: 10.1128/jvi.14.3.503-508.1974

Localization of Coliphage MS2 A-Protein

Linda K Curtiss 1, Robert G Krueger 2
PMCID: PMC355543  PMID: 4853028

Abstract

The purification of coliphage MS2 dinitrophenol (DNP) conjugates provided a system for localization of the single molecule of A-protein in the capsid of the MS2 phage particle. Three A-protein preparations isolated from unconjugated MS2, overconjugated DNP-MS2, and purified 78S DNP-MS2 were tested for the presence of covalently bound DNP. The binding characteristics to Dowex 1-X8 and rabbit anti-DNP bovine serum albumin (DNP-BSA) immunoglobulin G of the 78S DNP-MS2 and overconjugated DNP-MS2 A-protein preparations indicate that the A-protein is located on the surface of the phage particle where it can be covalently conjugated with hapten. Extensive enzymatic iodination of the A-protein of intact unconjugated MS2 substantiates this conclusion.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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