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The Physical Properties of a Protein Isolated from Bacteriophage φX174

Carusi, Edward A. and Sinsheimer, Robert L. (1963) The Physical Properties of a Protein Isolated from Bacteriophage φX174. Journal of Molecular Biology, 7 (4). pp. 388-400. ISSN 0022-2836. doi:10.1016/S0022-2836(63)80032-7.

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The protein moiety of bacteriophage φX174 can be dissociated into subunits of uniform molecular size by treatment with sodium dodecyl sulfate at elevated temperature and pH. Subsequent separation of protein from phage DNA may be effected by ammonium sulfate fractionation. About 60% of the protein of the starting material is recovered by this procedure. The physical state of the subunit is markedly dependent upon solvent conditions. On removal of detergent or lowering of pH the subunits aggregate. These aggregates may be dispersed by addition of detergent in alkaline (pH 10·5) solution.

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Additional Information:© 1963 Elsevier Ltd. Received 10 May 1963. This work was initiated while one of us (E. A. C.) was a fellow of the Jane Coffin Childs Memorial Fund for Medical Research, and has been supported in part by grants from the U.S. Public Health service (RG 6965). A preliminary report was presented at the April, 1961, meeting of the Federation of American Societies for Experimental Biology, Atlantic City, New Jersey.
Funding AgencyGrant Number
U.S. Public Health Service (USPHS)RG6965
Jane Coffin Childs Memorial Fund for Medical ResearchUNSPECIFIED
Issue or Number:4
Record Number:CaltechAUTHORS:20160616-110130577
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Official Citation:Edward A. Carusi, Robert L. Sinsheimer, The physical properties of a protein isolated from bacteriophage φX174, Journal of Molecular Biology, Volume 7, Issue 4, 1963, Pages 388-IN1, ISSN 0022-2836, (
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:67974
Deposited By: Ruth Sustaita
Deposited On:16 Jun 2016 21:49
Last Modified:11 Nov 2021 03:57

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