Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes.
Protein-protein and protein-salt interactions have been obtained for ovalbumin in solutions of ammonium sulfate and for lysozyme in solutions of ammonium sulfate, sodium chloride, potassium isothiocyanate, and potassium chloride. The two-body interactions between ovalbumin molecules in concentrated ammonium-sulfate solutions can be described by the DLVO potentials plus a potential that accounts for the decrease in free volume available to the protein due to the presence of the salt ions. The interaction between ovalbumin and ammonium sulfate is unfavorable, reflecting the kosmotropic nature of sulfate anions. Lysozyme-lysozyme interactions cannot be described by the above potentials because anion binding to lysozyme alters these interactions. Lysozyme-isothiocyanate complexes are strongly attractive due to electrostatic interactions resulting from bridging by the isothiocyanate ion. Lysozyme-lysozyme interactions in sulfate solutions are more repulsive than expected, possibly resulting from a larger excluded volume of a lysozyme-sulfate bound complex or perhaps, hydration forces between the lysozyme-sulfate complexes.
Curtis
R A
RA
Department of Chemical Engineering, University of California, Berkeley, Berkeley, California 94720, USA.
Prausnitz
J M
JM
Blanch
H W
HW
D000818:Animals; D001709:Biotechnology; D011232:Chemical Precipitation; D004573:Electrolytes; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D009113:Muramidase / Q000737:chemistry / Q000378:metabolism; D010047:Ovalbumin / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D012492:Salts / Q000737:chemistry; D012996:Solutions
D004573:Electrolytes; D046911:Macromolecular Substances; D011506:Proteins; D012492:Salts; D012996:Solutions; D010047:Ovalbumin; D009113:Muramidase