Bovine β-lactoglobulins in urea solution. Denaturation at pH 5.2 and 3.5

Ha, McKenzie; Gb, Ralston

doi:10.1021/bi00730a002

Cited by 18 publications

(10 citation statements)

References 33 publications

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“…Perhaps, the hydrophobic environment prevailing near pI and the close packing of protein material might have favored thiol/disulfide exchange reactions. However, it can not be totally excluded that some of the disulfide bonds were formed during incubation of the gel with the detergents, since denaturants like urea or SDS may lead to partial unfolding of proteins and promote thiol-disulfide interchange reactions (McKenzie and Ralston 1973;Shimada and Cheftel 1989;Howell 1992;Matsumura and Mori 1996;Hoffmann and others 1997). As the 5% ␤-Lg solution with pH 5.0 formed a gel upon the heat treatment, we have no exact information regarding the formation of building blocks prior to the formation of the ␤-Lg gel at pH 5.0.…”

Section: T He Formation and Maintenance Of A Protein Gel Net-mentioning

confidence: 99%

Involvement of Disulfide Bonds in Bovine β‐Lactoglobulin B Gels Set Thermally at Various pH

Otte

Zakora

Qvist

2000

Journal of Food Science

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To obtain information on forces important for maintenance of the structure of heat-set ␤-lactoglobulin gels, gels set from pure ␤-lactoglobulin at pH 3.0, 5.0, and 7.0 were solubilized in dissociating buffers, and solubilized material was characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and size exclusion high performance liquid chromatography. The gel formed at pH 7.0 was largely soluble in urea (or SDS), and this gel seemed to be built from covalently linked soluble aggregates, associating into a gel network mainly by strong noncovalent interactions. The gel set at pH 5.0 was solubilized only in the presence of a reducing agent, indicating that this gel structure was supported mainly by covalent disulfide bonds. The gel set at pH 3.0 was almost completely solubilized in SDS or urea without a reducing agent, showing the importance of noncovalent interactions in maintaining the gel structure.

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Section: T He Formation and Maintenance Of A Protein Gel Net-mentioning

confidence: 99%

Involvement of Disulfide Bonds in Bovine β‐Lactoglobulin B Gels Set Thermally at Various pH

Otte

Zakora

Qvist

2000

Journal of Food Science

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“…The refolding curves measured by the absorption changes at 295 and 270 nm are shown in Figure 4(b) and (c). The absorption increases with time during refolding at 295 nm, while at 270 nm it first decreases and then increases with time, indicating that the refolding is a complex reaction, involving a number of different kinetic intermediates (see McKenzie & Ralston, 1973). The refolding curves in Figure 4(b) and (c) also indicate that the refolding is not complete at 2500 s. We thus used manual mixing to induce the refolding of b-LGA, and the difference absorption spectra were recorded at different times after the refolding started.…”

Section: Kinetic Folding and Unfolding Curvesmentioning

confidence: 99%

The Burst-phase Intermediate in the Refolding of β-Lactoglobulin Studied by Stopped-flow Circular Dichroism and Absorption Spectroscopy

Kuwajima

Yamaya

Sugai

1996

Journal of Molecular Biology

126

107

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“…I n addition, there have been several papers on the thcrmodenaturation of P-lactoglobulin16-22 and the denaturation of PLG-A, B, C in urea solution at pH = 5.2 and 3.5. 23 Aside from the Raman spectraz4 and heat capacityz5 measurements, thc temperature dependence on partial molar volumesz6 of PLG has also been reported.…”

Section: Introductionmentioning

confidence: 99%

Self‐association of β‐lactoglobulin A in acid solution. I. Translational diffusion coefficients

et al. 1975

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SynopsisWe report measurements of the diffusion coefficient of p-lactoglobulin A (BLG-A) a t pH = 5.60 and 4.58 in 0.10 ionic strength acetate buffer by the techniques of analog photocurrent signal correlation and digital single-clipped photon correlation. At a concentration of 21 mg/ml and a pH of 4.58, the self-association of 0-lactoglobulin can be represented by a simple dimer-octamer equilibrium model. We determined the translational diffusion coefficient of the dimer and that of the octamer using the scattering results of Kumosinski and Timasheff in a dimer-octamer mixture. Our analysis shows that the dimer OLG-A does not change its size if the pH is varied from 5.60 to 4.58 and both species remain constant in size for temperature changes from 3.5" to 25°C Hydrodynamically, the octamers behave like closed-packed spheres with an effective radius of about 45 A according to the Stokes-Einstein relation.

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Bovine β-lactoglobulins in urea solution. Denaturation at pH 5.2 and 3.5

Cited by 18 publications

References 33 publications

Involvement of Disulfide Bonds in Bovine β‐Lactoglobulin B Gels Set Thermally at Various pH

Involvement of Disulfide Bonds in Bovine β‐Lactoglobulin B Gels Set Thermally at Various pH

The Burst-phase Intermediate in the Refolding of β-Lactoglobulin Studied by Stopped-flow Circular Dichroism and Absorption Spectroscopy

Self‐association of β‐lactoglobulin A in acid solution. I. Translational diffusion coefficients

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