Trichoplusia ni granulosis virus granulin: a phenol-soluble, phosphorylated protein.
AUTOR(ES)
Summers, M D
RESUMO
Trichoplusia ni granulosis virus granulin consists of one major polypeptide component with an estimated molecular weight of 28,000. The protein is phenol soluble, phosphorylated, and acidic. A protease activated by alkaline conditions is also associated with solubilized granulin preparations. If not properly inactivated, the protease will introduce extensive artifact into the protein giving rise to ambiguous and incorrect results as analyzed by SDS-polyacrylamide gel electrophoresis and peptide mapping. Procedures are documented for enzyme inactivation and the preparation of granulin in highly purified form for characterization.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=355708Documentos Relacionados
- Physical and Chemical Properties of Trichoplusia ni Granulosis Virus Granulin
- Carbohydrate Composition of the Phenol-soluble Lipopolysaccharides of Citrobacter freundii
- Phenol-Soluble Antigens from Mycobacterium kansasii, Mycobacterium gastri, and Mycobacterium marinum
- Characterization of novel, phenol-soluble polypeptides which confer rigidity to the sheath of Methanospirillum hungatei GP1.
- Membrane and protein interactions of a soluble form of the Semliki Forest virus fusion protein.
