Physical and chemical properties of Trichoplusia ni granulosis virus granulin.
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 beta-structure in the protein complex. The conversion of the beta-structure to alpha-helix with sodium lauryl sulfate and to a random coil state with strong alkaline treatment are observed.
D000596:Amino Acids / Q000032:analysis; D002499:Centrifugation, Density Gradient; D002849:Chromatography, Gas; D002854:Chromatography, Paper; D003124:Colorimetry; D004591:Electrophoresis, Polyacrylamide Gel; D007304:Insect Viruses / Q000032:analysis* / Q000302:isolation & purification; D008970:Molecular Weight; D009905:Optical Rotatory Dispersion; D010443:Peptide Chain Termination, Translational; D010455:Peptides / Q000032:analysis; D010761:Phosphorus Radioisotopes; D014461:Ultracentrifugation; D014764:Viral Proteins / Q000032:analysis*
D000596:Amino Acids; D010455:Peptides; D010761:Phosphorus Radioisotopes; D014764:Viral Proteins