Synthesis of the Major Bacteriophage f1 Coat Protein

AUTOR(ES)

Smilowitz, Henry

RESUMO

A method which allows one to follow the synthesis of the major f1 coat protein in normal, unirradiated f1-infected cells is reported. The N-terminal tryptic peptide of this protein, labeled with 14C-lysine, has a negative charge at pH 4.5 and is readily separated from the contaminating peptides of host cell proteins. This technique was used to study several aspects of the synthesis of the major f1 coat protein in infected cells.

Documentos Relacionados

• Bacteriophage f1 Infection: Fate of the Parental Major Coat Protein
• Minor coat protein composition and location of the A protein in bacteriophage f1 spheroids and I-forms.
• Effect of membrane-associated f1 bacteriophage coat protein upon the activity of Escherichia coli phosphatidylserine synthetase.
• Membrane biogenesis: cotranslational integration of the bacteriophage f1 coat protein into an Escherichia coli membrane fraction.
• Hexamer of bacteriophage f2 coat protein as a repressor of bacteriophage RNA polymerase synthesis.