PMID: 5257142Jun 1, 1969Paper

Effect of pressure on the apparent specific volume of proteins

Proceedings of the National Academy of Sciences of the United States of America
P F FaheyJ W Beams

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.

References

Jul 1, 1967·Proceedings of the National Academy of Sciences of the United States of America·G KegelesJ L Bethune
Oct 1, 1967·Proceedings of the National Academy of Sciences of the United States of America·R Josephs, W F Harrington
May 10, 1958·Nature·M A LAUFFERC C BRINTON
Aug 1, 1964·Proceedings of the National Academy of Sciences of the United States of America·D V ULRICHJ W BEAMS

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Citations

Aug 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·D W KupkeJ W Beams
Sep 11, 2008·Biotechnology and Bioengineering·Ryan L Crisman, Theodore W Randolph
Jan 25, 2003·Annual Review of Biophysics and Biomolecular Structure·Tigran V Chalikian
Aug 7, 1990·Biochemistry·K A Dill

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