EFFECT OF PRESSURE ON THE APPARENT SPECIFIC VOLUME OF PROTEINS
- 1 June 1969
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 63 (2) , 548-555
- https://doi.org/10.1073/pnas.63.2.548
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 degrees 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.Keywords
This publication has 11 references indexed in Scilit:
- An unusual pressure dependence for a reversibly associating protein system; sedimentation studies on myosin.Proceedings of the National Academy of Sciences, 1967
- PRESSURE AND HYDRATION EFFECTS ON CHEMICALLY REACTING SYSTEMS IN THE ULTRACENTRIFUGEProceedings of the National Academy of Sciences, 1967
- Sedimentation behavior of chemically reacting systems.Proceedings of the National Academy of Sciences, 1967
- The Nature of the Complexities in the Ribonuclease Conformational Transition and the Implications Regarding ClathratingJournal of the American Chemical Society, 1965
- Polymerization-Depolymerization of Tobacco Mosaic Virus Protein. IV. The Role of Water*Biochemistry, 1965
- Polymerization-Depolymerization of Tobacco Mosaic Virus Protein. III. Changes in Ionization and in Electrophoretic Mobility*Biochemistry, 1964
- AN IMPROVED MAGNETIC DENSITOMETER: THE PARTIAL SPECIFIC VOLUME OF RIBONUCLEASEProceedings of the National Academy of Sciences, 1964
- Alkaline Degradation of Turnip Yellow Mosaic Virus.* I. The Controlled Formation of Empty Protein ShellsBiochemistry, 1964
- Pollymerization–Depolymerizatic Tobacco Mosaic Virus ProteinNature, 1958
- Degradation of tobacco mosaic virus with acetic acidVirology, 1957