Abstract
The magnetic densimeter has been employed to measure the densities and apparent specific volumes of certain proteins in aqueous solutions as a function of pressure. The method gave values in satisfactory agreement with those found in the literature for aqueous electrolyte solutions. A change in apparent specific volume of the monomeric proteins, ribonuclease and turnip yellow mosaic virus and its capsid protein, at pressures up to 400 atmospheres at 20°C was not observed within the precision of the measurements. Also, no change in the apparent specific volume of tobacco mosaic virus protein was observed as a function of these pressures whether the protein was predominantly in the polymerized or unpolymerized state. The magnetic densimeter was found to be a convenient instrument for measuring compressibilities of very small samples of solutions.
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Selected References
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- ANSEVIN A. T., STEVENS C. L., LAUFFER M. A. POLYMERIZATION-DEPOLYMERIZATION OF TOBACCO MOSAIC VIRUS PROTEIN. 3. CHANGES IN IONIZATION AND IN ELECTROPHORETIC MOBILITY. Biochemistry. 1964 Oct;3:1512–1518. doi: 10.1021/bi00898a021. [DOI] [PubMed] [Google Scholar]
- BRANDTS J. F. THE NATURE OF THE COMPLEXITIES IN THE RIBONUCLEASE CONFORMATIONAL TRANSITION AND THE IMPLICATIONS REGARDING CLATHRATING. J Am Chem Soc. 1965 Jun 20;87:2759–2760. doi: 10.1021/ja01090a043. [DOI] [PubMed] [Google Scholar]
- Banerjee K., Lauffer M. A. Polymerization--depolymerization of tobacco mosaic virus protein. VI. Osmotic pressure studies of early stages of polymerization. Biochemistry. 1966 Jun;5(6):1957–1964. doi: 10.1021/bi00870a024. [DOI] [PubMed] [Google Scholar]
- FRAENKEL-CONRAT H. Degradation of tobacco mosaic virus with acetic acid. Virology. 1957 Aug;4(1):1–4. doi: 10.1016/0042-6822(57)90038-7. [DOI] [PubMed] [Google Scholar]
- Josephs R., Harrington W. F. An unusual pressure dependence for a reversibly associating protein system; sedimentation studies on myosin. Proc Natl Acad Sci U S A. 1967 Oct;58(4):1587–1594. doi: 10.1073/pnas.58.4.1587. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KAPER J. M. ALKALINE DEGRADATION OF TURNIP YELLOW MOSAIC VIRUS. I. THE CONTROLLED FORMATION OF EMPTY PROTEIN SHELLS. Biochemistry. 1964 Apr;3:486–493. doi: 10.1021/bi00892a004. [DOI] [PubMed] [Google Scholar]
- Kegeles G., Rhodes L., Bethune J. L. Sedimentation behavior of chemically reacting systems. Proc Natl Acad Sci U S A. 1967 Jul;58(1):45–51. doi: 10.1073/pnas.58.1.45. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LAUFFER M. A., ANSEVIN A. T., CARTWRIGHT T. E., BRINTON C. C., Jr Polymerization-depolymerization of tobacco mosaic virus protein. Nature. 1958 May 10;181(4619):1338–1339. doi: 10.1038/1811338b0. [DOI] [PubMed] [Google Scholar]
- STEVENS C. L., LAUFFER M. A. POLYMERIZATION-DEPOLYMERIZATION OF TOBACCO MOSAIC VIRUS PROTEIN. IV. THE ROLE OF WATER. Biochemistry. 1965 Jan;4:31–37. doi: 10.1021/bi00877a007. [DOI] [PubMed] [Google Scholar]
- Teneyck L. F., Kauzmann W. Pressure and hydration effects on chemically reacting systems in the ultracentrifuge. Proc Natl Acad Sci U S A. 1967 Sep;58(3):888–894. doi: 10.1073/pnas.58.3.888. [DOI] [PMC free article] [PubMed] [Google Scholar]
- ULRICH D. V., KUPKE D. W., BEAMS J. W. AN IMPROVED MAGNETIC DENSITOMETER: THE PARTIAL SPECIFIC VOLUME OF RIBONUCLEASE. Proc Natl Acad Sci U S A. 1964 Aug;52:349–356. doi: 10.1073/pnas.52.2.349. [DOI] [PMC free article] [PubMed] [Google Scholar]