Construction and performance of the brice photoelectric differential refractometer

Pittz, Eugene P.; Bablouzian, B.

doi:10.1016/0003-2697(73)90129-2

Cited by 6 publications

(1 citation statement)

References 2 publications

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“…Refractive Index Increments. Refractive index increments of RNase A were measured on a photoelectric differential refractometer at 436 nm and 25 °C (Pittz and Bablouzian, 1973). For measurements of the refractive index increment at identical chemical potentials of solvent components in the protein solution and the reference solvent, (órt/dC2)7-,M1,M3, the ribonuclease A solution was first brought to dialysis equilibrium with the solvent; the dialyzed protein and dialysates were then introduced into the two compartments of the differential cell.…”

Section: Methodsmentioning

confidence: 99%

Interaction of ribonuclease A with aqueous 2-methyl-2,4-pentanediol at pH 5.8

Pittz¹,

Timasheff²

1978

Biochemistry

137

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The interactions between ribonuclease A and solvent components in aqueous 2-methyl-2,4-pentanediol (MPD) have been investigated by differential refractometry and light scattering at pH 5.8, i.e., conditions similar to those used to crystallize the protein from this solvent system. Application of multicomponent thermodynamic theory shows that, at all solvent compositions up to 50% (v/v) MPD, the protein is preferentially hydrated; i.e., addition of ribonuclease to the mixed solvent leads to an increase in the chemical potential of MPD. This unfavorable thermodynamic interaction leads to phase separation, probably caused by local salting out of the MPD by the charges on the surface of the protein molecule. A parallel examination by circular dichroism (CD) has shown that the CD spectrum of ribonuclease in 50% MPD is indistinguishable from that in dilute buffer.

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Section: Methodsmentioning

confidence: 99%

Interaction of ribonuclease A with aqueous 2-methyl-2,4-pentanediol at pH 5.8

Pittz¹,

Timasheff²

1978

Biochemistry

137

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Light‐scattering properties of sodium and magnesium alginate

Dingsøyr¹,

Smidsrød²

1977

Brit. Poly. J.

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The weight-average molecular weight of a fraction of magnesium alginate was found by light-scattering to be identical within experimental error to that of the corresponding fraction of sodium alginate. The difference in the charge density of sodium and magnes: ium alginate had no detectable effect on their measured radii of gyration at ionic strength 0.1, but had a great effect on the second virial coefficient of the solutions. The Orfino-Flory theory was used to calculate expansion factors, a, from the second virial coefficients, assuming that these were composed of two terms, one due to polymersolvent interaction and one due to electrostatic interactions. .A comparison with a-values obtained from viscosity data at different ionic strengths suggested that alginate is soluble in water because of electrostatic stabilisation and not because of a favourable polymerwater interaction.

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Human spectrin. I. A classical light scattering study

Elgsaeter

1978

Biochimica et Biophysica Acta (BBA) - Protein Structure

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Construction and performance of the brice photoelectric differential refractometer

Cited by 6 publications

References 2 publications

Interaction of ribonuclease A with aqueous 2-methyl-2,4-pentanediol at pH 5.8

Interaction of ribonuclease A with aqueous 2-methyl-2,4-pentanediol at pH 5.8

Light‐scattering properties of sodium and magnesium alginate

Human spectrin. I. A classical light scattering study

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