Osmotically unresponsive water fraction on proteins: Non-ideal osmotic pressure of bovine serum albumin as a function of pH and salt concentration

Gary D. Fullerton; Kalpana M. Kanal; Ivan L. Cameron

doi:10.1016/j.cellbi.2005.11.001

Osmotically unresponsive water fraction on proteins: Non-ideal osmotic pressure of bovine serum albumin as a function of pH and salt concentration

Gary D. Fullerton, Kalpana M. Kanal, Ivan L. Cameron

Department of Cell Systems & Anatomy

Research output: Contribution to journal › Article › peer-review

30 Scopus citations

Abstract

How much does protein-associated water differ in colligative properties (freezing point, boiling point, vapor pressure and osmotic behavior) from pure bulk water? This question was approached by studying the globular protein bovine serum albumin (BSA), using changes in pH and salt concentration to alter its native structural conformation and state of aggregation. BSA osmotic pressure was investigated experimentally and analyzed using the molecular model of Fullerton et al. [Biochem Cell Biol 1992;70(12):1325]. Analysis yielded both the extent of osmotically unresponsive water (OUW) and the effective molecular weight values of the membrane-impermeable BSA solute. Manipulation of BSA conformation and aggregation by membrane-penetrating cosolutes show that alterations in pH and salt concentration change the amount of bulk water that escapes into BSA from a minimum of 1.4 to a maximum of 11.7 g water per g dry mass BSA.

Original language	English (US)
Pages (from-to)	86-92
Number of pages	7
Journal	Cell Biology International
Volume	30
Issue number	1
DOIs	https://doi.org/10.1016/j.cellbi.2005.11.001
State	Published - Jan 2006

Keywords

Interfacial water
Osmosis
Osmotically unresponsive water
Protein conformation

ASJC Scopus subject areas

Cell Biology

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10.1016/j.cellbi.2005.11.001

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abstract = "How much does protein-associated water differ in colligative properties (freezing point, boiling point, vapor pressure and osmotic behavior) from pure bulk water? This question was approached by studying the globular protein bovine serum albumin (BSA), using changes in pH and salt concentration to alter its native structural conformation and state of aggregation. BSA osmotic pressure was investigated experimentally and analyzed using the molecular model of Fullerton et al. [Biochem Cell Biol 1992;70(12):1325]. Analysis yielded both the extent of osmotically unresponsive water (OUW) and the effective molecular weight values of the membrane-impermeable BSA solute. Manipulation of BSA conformation and aggregation by membrane-penetrating cosolutes show that alterations in pH and salt concentration change the amount of bulk water that escapes into BSA from a minimum of 1.4 to a maximum of 11.7 g water per g dry mass BSA.",

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AU - Cameron, Ivan L.

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AB - How much does protein-associated water differ in colligative properties (freezing point, boiling point, vapor pressure and osmotic behavior) from pure bulk water? This question was approached by studying the globular protein bovine serum albumin (BSA), using changes in pH and salt concentration to alter its native structural conformation and state of aggregation. BSA osmotic pressure was investigated experimentally and analyzed using the molecular model of Fullerton et al. [Biochem Cell Biol 1992;70(12):1325]. Analysis yielded both the extent of osmotically unresponsive water (OUW) and the effective molecular weight values of the membrane-impermeable BSA solute. Manipulation of BSA conformation and aggregation by membrane-penetrating cosolutes show that alterations in pH and salt concentration change the amount of bulk water that escapes into BSA from a minimum of 1.4 to a maximum of 11.7 g water per g dry mass BSA.

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Osmotically unresponsive water fraction on proteins: Non-ideal osmotic pressure of bovine serum albumin as a function of pH and salt concentration

Abstract

Keywords

ASJC Scopus subject areas

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