STUDIES ON PHAGE COAT PROTEIN
I. CHEMICAL ANALYSIS OF FRACTION 3
1979 Volume 29 Issue 2 Pages 141-148
Details
1979 Volume 29 Issue 2 Pages 141-148
The proteins of Salmonella phage P22 were extracted with acetic acid and fractionated on a DEAE-cellulose column. The fractionated proteins were named Fraction 1 (F1), Fraction 2 (F2) and Fraction 3 (F3). F3 protein was suggested to be a main component related to the production of antibody. It was investigated for biochemical characteristics.
1. When P22 protein (P22P) was fractionated on a DEAE-cellulose column with 0.001-0.02M phosphate buffer, a large yield was obtained after the pH of the sample was regulated with 0.001M phosphate buffer before fractionation.
2. The isolated F3 fraction was treated with trypsin and developed by two-dimensional paper chromatography. Sixteen peptides were detected with ninhydrin solution.
3. The N-terminal amino acid sequence of the fraction was determined by the dansyl method. It was suggested that the N-terminal might be the Val-Val or Val-Ile sequence.
4. After citraconylation and tryptic digestion, the fraction was applied to Dowex 50X2 with pyridinium acetate buffer. By the fluorescamine method 9-18 peaks were detected. With 10 of these peaks the N-terminal sequence was determined by the dansyl method.
