Studies on the Phage Protein. (I)

Abstract

Phage P22 was purified by the concentration in vacuo, ultracentrifugation and ECTEOLA-cellulose column chromatography from its lysate. Yield of the purified Phage was 10ml (1013 phages per ml) obtained from original lysate of 3l. The protein preparation was carried out by acetic acid degradation and its yield was 10ml (2.2mg/ml) from 50ml of the purified phage. The protein showed the mobility of 8.293mm in the electrophoresis on cellulose acetate strip, while the mobilities of the components of rabbit serum were 23.771, 16.271, 10.771 and 8.443mm, respectively. The values of the host flagella and host protein were 3.650mm and 0.000mm, respectively. Consequently, the phage protein obtained was of a single component and differed from the host protein. According to the amino acid analysis, histidine, leucine, lysine, and phenylalanine were found more abundantly in phage protein than in host protein. In general, alanine, aspartic acid, glutamic acid, glycine and leucine were predominant of the other amino acids. Proline was found only in the phage protein and was not in the host protein.