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. 1973 Nov;12(5):1092–1103. doi: 10.1128/jvi.12.5.1092-1103.1973

Physical and Chemical Properties of Trichoplusia ni Granulosis Virus Granulin

Max D Summers 1, Kohji Egawa 2
PMCID: PMC356741  PMID: 4765397

Abstract

The protein solubilized from the proteinic crystalline structure surrounding the granulosis virus of Trichoplusia ni by use of a carbonate buffer (pH 10.7) gives a major component, as analyzed by ultracentrifugation, with a molecular weight of 180,000. This protein has heterogeneous subunit structure as demonstrated by estimates of molecular weights by use of gel electrophoresis, amino-, and carboxy-terminal analyses, and peptide mapping of enzyme digests of the protein. The amino acid composition shows that the protein is acidic with a high percentage of amino acids with hydrophobic side groups. Optical rotatory dispersion studies reveal the presence of β-structure in the protein complex. The conversion of the β-structure to α-helix with sodium lauryl sulfate and to a random coil state with strong alkaline treatment are observed.

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Selected References

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