Published October 1963
| public
Journal Article
The Physical Properties of a Protein Isolated from Bacteriophage φX174
- Creators
- Carusi, Edward A.
- Sinsheimer, Robert L.
Abstract
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.
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.Additional details
- Eprint ID
- 67974
- DOI
- 10.1016/S0022-2836(63)80032-7
- Resolver ID
- CaltechAUTHORS:20160616-110130577
- RG6965
- U.S. Public Health Service (USPHS)
- Jane Coffin Childs Memorial Fund for Medical Research
- Created
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2016-06-16Created from EPrint's datestamp field
- Updated
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2021-11-11Created from EPrint's last_modified field