The Isolation and Characterization of the Tryptic Peptides from the f₂ Bacteriophage Coat Protein

From the ¹ From the Department of Biochemistry, Yale University, New Haven, Connecticut, and The Rockefeller University, New York, New York 10021

Tryptic digestion of the f₂ coat protein produced 10 peptides and free lysine. Peptides which were soluble in 0.2 m pyridine acetate buffer, pH 3.1, were separated on columns of Dowex 50-X4. Peptides insoluble at this pH were fractionated by gel filtration on Sephadex G-50 with the use of 88% formic acid or by chromatography on diethylaminoethyl Sephadex in 8 m urea. Amino- and carboxyl-terminal analyses were performed on the protein and the peptides. The NH₂-terminal residue of the protein is alanine and the COOH-terminal amino acid is tyrosine. The tryptic peptides which occupy the terminal positions in the protein were identified. The sum of amino acids in the tryptic peptides was estimated to be 129, and also the amino acid composition of the protein indicated 129 residues.

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