Physicochemical studies on bovine eye lens proteins II. Comparative physical study of the low-molecular-weight α-crystallins from calf lens cortical and nuclear fiber cells

Coopman, Serge; Block, Jan De; Aerts, Tony; Peeters, Wim; Moëns, Luc; Clauwaert, J.

doi:10.1016/0014-4835(84)90124-6

Cited by 11 publications

(1 citation statement)

References 31 publications

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“…When considering the polydispersity in the results of light scattering by a-crystallin proteins in different ionic strength, we have to known 8. This can be calculated from the experimental molar mass M and hydrodynamic radius a (see Table 2) and the values of Mo = 600,000 and ao = 8.5 nm (Coopman et al, 1984;Tardieu et al, 1986;Schurterberger and Augusteyn, 1991;Augusteyn et al, 1992). We obtained a value 8 = 0.14 + 0.03, which results in a correction of factor of 1.19 for the hydrodynamic volume 4.…”

Section: Biophysical Journalmentioning

confidence: 99%

Light scattering by bovine alpha-crystallin proteins in solution: hydrodynamic structure and interparticle interaction

Xia

Aerts

Donceel

et al. 1994

Biophysical Journal

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We have studied diluted bovine eye lens alpha-crystallin solutions by using light scattering. The protein particles were modeled as hard spheres, showing electrostatic repulsion, due to surplus electric charges, and weak attractive interaction. The repulsive potential VR is defined by the radius of the particles, the Debye length kappa-1, and the number of charges at the Gouy layer; the attractive potential has been described by the London-van der Waals potential and is defined by the Hamaker constant A. We have used the diluted gas approximation and the one component macrofluid model to relate the experimental static factor Ki to the theoretical expression of the interaction potential V(x). This resulted in a Hamaker constant A of 0.06 +/- 0.01 KBT and an effective charge q ranging from 18 +/- 1 at low ionic strength (omega = 0.0022 M) to 50 +/- 5 at high ionic strength (omega = 0.1472 M).

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Section: Biophysical Journalmentioning

confidence: 99%

Light scattering by bovine alpha-crystallin proteins in solution: hydrodynamic structure and interparticle interaction

Xia

Aerts

Donceel

et al. 1994

Biophysical Journal

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Interaction of detergents with bovine lens α-crystallin: evidence for an oligomeric structure based on amphiphilic interactions

Aerts

Clauwaert

Haezebrouck

et al. 1997

European Biophysics Journal

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We have studied the quaternary structure of alpha-crystallin in the presence of increasing concentrations of amphiphilic and neutral detergents using gel filtration, light-scattering, boundary and equilibrium sedimentation. We observed a continuous reduction of the molar mass of the polymeric alpha-crystallin on increasing the concentration of sodium dodecyl sulphate from 0.1 mM to 5 mM, ending up with the monomeric peptides. Dodecyltrimethylammonium bromide also disrupts the oligomeric structure of alpha-crystallin but the interaction appears to be cooperative: in the sharp transition region (for a 1 mg/ml protein solution) from 3 to 8 mM of the detergent, only the native protein and a mixture of monomeric and dimeric peptide-DTAB complexes can be observed. Concomitant studies of the circular dichroism in the far UV revealed a substantial decrease of the beta-sheet and increase of the alpha-helix secondary structure. The latter can be related to the presence of amphiphilic polypeptide sequences in the constituent alpha A and alpha B peptides. These studies reveal for the first time a direct relation between changes in the secondary structure of the alpha A and alpha B peptides and the formation of the oligomeric alpha-crystallin structure: the binding of the amphiphilic detergent reduces the beta-sheet content, induces the formation of alpha-helix secondary structure and reduces the tendency of the peptide to form large aggregates. The different mechanisms for reducing the oligomeric size by anionic and cationic detergents with identical apolar parts stresses the importance of charge interactions. Our findings support some aspects of the micelle model of alpha-crystallin and can be related to its chaperone activity.

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High-molecular-weight protein aggregates of calf and cow lens: Spectroscopic evaluation

Messmer

Chakrabarti

1988

Experimental Eye Research

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Physicochemical studies on bovine eye lens proteins II. Comparative physical study of the low-molecular-weight α-crystallins from calf lens cortical and nuclear fiber cells

Cited by 11 publications

References 31 publications

Light scattering by bovine alpha-crystallin proteins in solution: hydrodynamic structure and interparticle interaction

Light scattering by bovine alpha-crystallin proteins in solution: hydrodynamic structure and interparticle interaction

Interaction of detergents with bovine lens α-crystallin: evidence for an oligomeric structure based on amphiphilic interactions

High-molecular-weight protein aggregates of calf and cow lens: Spectroscopic evaluation

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