抄録
Studies on the Phage Protein. (II)
Immunresponse of P22 Phage protein.
Michko HORIKOSHI and Kiyoaki KAMIJO
TISSUE CULTURE LAB.,
Juntendo University School of Medicine
Coat protein of phage P22 was extracted by the acetic acid method of Fraenkel-Conrat and its immunological activities were examined in antibody production, blocking power, immunoelectrophoresis and gel-diffusion precipitation. The results obtained were summarized as follows.
1. The coat protein was obtained by the acetic acid degradation of P22 phage and designated as P22-protein.
2. The P22-protein showed the complete antigenicity both in precipitin and neutralizing antibody production.
3. Anti-P22-protein serum neutralized the original phage P22.
4. Titers of the neutralizing antibodies (K values) were 220.4, 90.5 and 87.4 for anti-P22, anti-P22-protein and anti-lysate sera, respectively.
5. The P22-protein blocked the neutralizing effect of the anti-P22 serum.
6. Both in immunoelectrophoresis and gel-diffusion precipitation, only single precipitation line was shown, suggesting that the P22-protein would composed of single component. Considering the morphological structre of the phage, however, it may be expected more complexity in its components.
The investigation is now in progress with more sensitive method on this problem.
