Capsid Polypeptides of Mouse Elberfeld Virus I. Amino Acid Compositions and Molar Ratios in the Virion
AUTOR(ES)
Stoltzfus, C. Martin
RESUMO
The four major polypeptide chains (alpha, beta, gamma, delta) constituting the capsid protein of mouse Elberfeld (ME) virus were isolated by preparative electrophoresis on polyacrylamide gels, and the amino acid composition of each chain was determined. In addition, the molecular weights of the smallest chains of ME virus, mengovirus, and poliovirus, which had previously been determined by gel electrophoretic methods, were redetermined by gel filtration chromatography in 6 m guanidine hydrochloride. Each was found to have a molecular weight about 7,300. Using the reevaluated molecular weights and the known amino acid compositions of the chains, the molar ratio of each chain in the ME virion was determined by quantitative analysis of the distribution of radioactivity in the electrophoretically separated chains of virus which had been specifically radiolabeled with leucine or with methionine. Equimolar proportions of all four chains were found in the virion.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=356473Documentos Relacionados
- N-terminal amino acid sequences and amino acid compositions of the Spirochaeta aurantia flagellar filament polypeptides.
- Proteins of hepatitis B surface antigen: amino acid compositions of the major polypeptides.
- THE STRUCTURE OF MOUSE-ELBERFELD VIRUS: A MODEL*
- A Single Amino Acid Mutation in the Carnation Ringspot Virus Capsid Protein Allows Virion Formation but Prevents Systemic Infection
- Partial molar rotatory powers and optical activity in proteins and polypeptides. I. The fully extended chain and the antiparallel beta-pleated sheet.
