Purification, Properties and Assembly of the Neck‐Appendage Protein of the Bacillus subtilis Phage φ 29
- 1 July 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 117 (3) , 499-505
- https://doi.org/10.1111/j.1432-1033.1981.tb06365.x
Abstract
The purification of the neck appendage protein of .vphi.29,p12*, which is involved in the adsorption of the phage to B. subtilis, is described. The purified native protein is in a dimeric form and can be assembled, in vitro, onto purified 12- particles that lack the neck appendages, suggesting that the incorporation of p12* to the rest of the phage structure is a self-assembly process. The assembly of protein p12* in vitro follows cooperative kinetics and it occurs with an efficiency of about 4%.This publication has 31 references indexed in Scilit:
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