The solubility dependence of canavalin on pH and temperature

DeMattei, R.C.; Feigelson, R. S.

doi:10.1016/0022-0248(91)90863-z

Cited by 36 publications

(20 citation statements)

References 11 publications

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“…Even so, extensive solubility data taking into account all these factors is only available for the model system hen egg white lysozyme (HEWL) [1][2][3][4][5][6][7][8][9]. Other protein solubilities that have been studied in detail for a specific set of conditions include: glucose isomerase (GI) [10][11][12], thaumatin [13], BTPI [14,15], concanavalin A [16], canavalin [17], insulin [18], human hemoglobin C [19] and ovalbumin [20]. Although the level of precision in these measurements is frequently not very high the obtained solubility data are very useful for setting up screening conditions for crystallization or explaining qualitative growth observations.…”

Section: Introductionmentioning

confidence: 99%

Precise protein solubility determination by Laser confocal differential interference contrast microscopy

Driessche¹,

Gavira²,

Lopez³

et al. 2009

Journal of Crystal Growth

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Section: Introductionmentioning

confidence: 99%

Precise protein solubility determination by Laser confocal differential interference contrast microscopy

Driessche¹,

Gavira²,

Lopez³

et al. 2009

Journal of Crystal Growth

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“…3 Protein phase separations can also be the cause of human diseases, such as cataract 4 or sickle cell disease. 5 Despite their fundamental importance, phase diagrams of only a few proteins have been studied: insulin, 6 fibrinogen, 7 γ-crystallin, 8 lysozyme, 4,9-12 concanavalin, 13 canavalin, 14 R-amylase, 15,16 collagenase, 17 bovine pancreatic trypsin inhibitor (BPTI), 16,18 apoferritin, 19 endoglucanase A, 20 and the photochemical reaction center from Rhodobacter sphaeroides Y. 21 Recently, there has been a renewed enthusiasm for phasetransition studies of colloids 22 and proteins [22][23][24][25][26][27] due to advances in experimental and computational technologies.…”

Section: Introductionmentioning

confidence: 99%

Exploring Bovine Pancreatic Trypsin Inhibitor Phase Transitions

et al. 2006

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This paper presents an investigation of the phase diagram of BPTI (bovine pancreatic trypsin inhibitor)/350 mM KSCN at pH 4.9 by direct observation and numerical simulations. We report optical microscopy and light and X-ray scattering experiments coupled with theoretical data analysis using numerical tools. The phase diagram is thoroughly determined, as a function of temperature. Two polymorphs are observed by video microscopy and their solubility measured. In this phase diagram, the liquid-liquid phase separation (LLPS) is metastable with respect to the solid-liquid phase separation. Above the T L-L boundary curve, solutions are composed of a mixture of BPTI monomers and decamers. Attractive interactions are stronger between decamers than between monomers. Below the T L-L boundary curve, the dense phase is highly concentrated in protein and composed of BPTI decamers alone. Thus, the driving force for liquid-liquid or liquid-solid phase separation is the attraction between decamers at low pH. The structure factors of the dense phases are characteristic of repulsive dense phases because of a hard sphere repulsion core, meaning that in the dense phase proteins are actually in contact (interparticle distance of 53 Å). In agreement with the Oswald rule of stages, LLPS occurs prior to and impedes the solid nucleation.

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“…G. Feher and his coworkers (18,19) have produced a pioneering theoretical and experimental analysis of the kinetic factors that control the growth of crystals and amorphous precipitates. The equilibrium phase boundaries have more recently been studied in the cases of lysozyme (20)(21)(22), concanavalin A (23), and canavalin (24). The phase boundary between a solution phase and a polymerized gel phase of deoxyhemoglobin S has also been studied, and the enthalpy change accompanying this phase transition has been estimated (25)(26)(27)).…”

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confidence: 99%

Solid-liquid phase boundaries of lens protein solutions.

Berland

Thurston

Kondo

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

161

103

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We report measurement of the solid-liquid phase boundary, or liquidus line, for aqueous solutions of three pure calf y6-crystallin proteins: y$I, yHIa, and yIHIb. We also studied the liquidus line for solutions of native yIV-crystallin calf lens protein, which consists of 85% yIVa/15% yIVb. In all four proteins the liquidus phase boundaries lie higher in temperature than the previously determined liquid-lquid coexistence curves. Thus, over the range of concentration and temperature for which liquid-liquid phase separation occurs, the coexistence of a protein crystal phase with a protein liquid solution phase is thermodynamically stable relative to the metastable separated liquid phases. The location ofthe liquidus lines clearly divides these four crystallin proteins into two groups: those in which liquidus lines flatten at temperatures >70rC: yMa and yIV, and those in which liquidus lines flatten at temperatures <500C: yll and -yIlb. We have analyzed the form of the liquidus lines by using specific choices for the structures of the Gibbs free energy in solution and solid phases. By applying the thermodynamic conditions for equilibrium between the two phases to the resulting chemical potentials, we can estimate the temperature-dependent free energy change upon binding of protein and water into the solid phase.Maintenance ofthe lens proteins in a single homogenous fluid phase is an essential condition for transparency of the eye lens (1, 2). Consequently, we previously investigated the location of the coexistence curve (3-5) for liquid-liquid phase separation for four pure calf y-crystallin protein solutions. In those studies, preliminary findings at a few points in the phase diagram suggested that the coexistence curve for solid-liquid phase equilibrium might be higher in temperature than the liquid-liquid coexistence curve (4, 5). We, therefore, undertook the present systematic investigation of the location of the solid-liquid coexistence curve for three pure lens crystallin proteins 'yII, yIIIa, and yIIIb, as well as for native 'yIV protein, which is a mixture of yIVa and yIVb in relative proportion of 85% to 15%, respectively, by number. We report here the measurement for each protein of the ascending limb of the solid-liquid coexistence curve. This limb is called the liquidus line; it is defined as the locus of points in the concentration (c) and temperature (T) plane that corresponds to equilibrium between protein crystals and an aqueous liquid solution of the same protein having concentration c. This locus can be designated by TL(c), or alternatively cL(T). At fixed temperature T, the concentration CL is the solubility of the protein in aqueous solution. The descending limb ofthe solid-liquid coexistence curve is called the solidus line c5(T), and it is the locus of points showing the protein concentration in the solid phase for each temperature T. For cL(T) < c < c,(T), the equilibrium state of the solution consists of a mixture of protein crystals of protein concentration c5(T) and aqueous liquid ...

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The solubility dependence of canavalin on pH and temperature

Cited by 36 publications

References 11 publications

Precise protein solubility determination by Laser confocal differential interference contrast microscopy

Precise protein solubility determination by Laser confocal differential interference contrast microscopy

Exploring Bovine Pancreatic Trypsin Inhibitor Phase Transitions

Solid-liquid phase boundaries of lens protein solutions.

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