EFFECT OF PRESSURE ON THE APPARENT SPECIFIC VOLUME OF PROTEINS*
AUTOR(ES)
Fahey, Paul F.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=223598Documentos Relacionados
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