Structural basis of eye lens transparency: Light scattering by concentrated solutions of bovine α-crystallin proteins

Biophysical Journal

Volumn 71, Issue 5, 1996, Pages 2815-2822

  Xia, Jia Zhi ^a,b   Wang, Qinghua ^a,c   Tatarkova, Sveta ^a,d   Aerts, Tony ^a   Clauwaert, Julius ^a  

^a UNIVERSITY OF ANTWERP   (Belgium)

^b QUEEN S UNIVERSITY   (Canada)

^c HOSPITAL FOR SICK CHILDREN   (Canada)

^d SARATOV STATE UNIVERSITY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; LENS PROTEIN;

ARTICLE; DIFFUSION COEFFICIENT; HYDRODYNAMICS; LENS; LIGHT SCATTERING; MODEL;

BOVINAE;

EID: 0029910042     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79477-8     Document Type: Article

References (43)

1. Aerts, A., Q. H. Wang, S. Tatarkova, and J. Clauwaert. 1995. Physical-chemical characterization of the different individual cortical alfacrystallin fractions from bovine lenses. Colloid Polym. Sci. 99:94-100.
2. Andries, C., H. Backhovens, J. Clauwaert, J. De Block, F. De Voeght, and C. Dhont. 1982. Physical-chemical studies on bovine eye lens proteins. I. Light-scattering and viscosity studies of low-molecular weight α-crystallin isolated from adult and embryonic bovine lenses. Exp. Eye Res. 34:239-255.
3. Andries, C., W. Guedens, J. Clauwaert, H. Geerts. 1983. Photon and fluorescence correlation spectroscopy and light scattering of eye-lens proteins at moderate concentrations. Biophys. J. 43:345-354.
4. Atchison, D. A., and G. Smith. 1995. Continuous gradient index and shell models of the human lens. Vision Res. 35:2529-2538.
5. Augusteyn, R. C., E. M. Parkhill, and A. Stevens. 1992. The effects of isolation buffers on the properties of α-crystallin. Exp. Eye Res. 54: 219-228.
6. Bender, T. M. R., R. J. Lewis, and R. Pecora. 1986. Absolute Rayleigh ratios of four solvents at 488 nm. Macromolecules. 19:244-245.
7. Benedek, G. B. 1971. Theory of transparency of the eye. Appl. Optics. 10:459-473.
8. Bloemendal, H. 1981. Molecular and Cellular Biology of the Eye Lens. John Wiley and Sons, New York. p. 469.
9. Braig, K., Z. Otwinowski, R. Hegde, D. C. Boisvert, A. Joachimiak, A. L. Horwich, and P. B. Sigler. 1994. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å. Nature. 371:578-586.
10. Darragh, A. J., D. J. Garrick, P. J. Moughan, and W. H. Hendriks. 1996. Correction for amino acid loss during acid hydrolysis of a purified protein. Anal. Biochem. 236:199-207.
11. Delaye, M., and A. Gromiec. 1983. Mutual diffusion of crystallin proteins at finite concentrations: a light-scattering study. Biopolymers. 22: 1203-1221.
12. Delaye, M., and A. Tardieu. 1983. Short-range order of crystallin proteins accounts for eye lens transparency. Nature. 302:415-417.
13. Goodwin, T. W., and R. A. Morton. 1946. The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem. J. 40: 628-632.
14. Groenen, P., J. T. A., K. B. Merck, W. W. De Jong, and H. Bloemendal. 1994. Structure and modifications of the junior chaperone α-crystallin. From lens transparency to molecular pathology. Eur. J. Biochem. 225: 1-19.
15. Hayter, J. B. and J. Penfold. 1981. An analytical structure factor for macroion solutions. Mol. Phys. 42:109-118.
16. Ishihama, A., T. Ikeuchi, A. Matsumoto, and S. Yamamoto. 1976. A novel adenosine triphosphatase isolated from RNA polymerase preparations of Escherichia Coli. J. Biochem. 79:927-936.
17. Jagger, W. S. 1992. The optics of the spherical fish lens. Vision Res. 32:1271-1284.
18. Kröger, R. H. H., M. C. W. Campbell, R. Munger, and R. D. Femalds. 1994. Refractive index distribution and spherical aberration in the crystalline lens of the african cichlid fish Haplochromoris burtoni. Vision Res. 34:1815-1822.
19. Lechner, M. D., and W. Mächtle. 1991. A new procedure for the determination of the molar mass distribution of polymers in solution from sedimentation equilibrium. Colloid Polym. Sci. 86:62-69.
20. Ohshima, H., T. W. Healy, and L. R. White. 1982. Accurate analytical expression for the surface charge density/surface potential relationship and double-layer potential distribution for a spherical colloidal particle. J. Colloid Interface Sci. 90:17-26.
21. Pace, N. C., F. Vajdos, L. Fee, G. Grimsley, and T. Gray. 1995. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4:2411-2423.
22. Provencher, S. W. 1982a. Contin: a general purpose constrained regularization program for inverting noisy linear algebraic and integral equations. Comput. Phys. Commun. 27:229-242.
23. Provencher, S. W. 1982b. A constrained regularization method for inverting data represented by linear algebraic or integral equations. Comput. Phys. Commun. 27:213-227.
24. Pusey. P. N., H. M. Fijnaut, and A. Vrij. 1982. Mode amplitudes in dynamic light scattering by concentrated liquid suspensions of polydisperse hard spheres. J. Chem. Phys. 77:4270-4281.
25. Ree, H. F., and G. W. Hoover. 1967. Seventh virial coefficients for hard spheres and hard disks. J. Chem. Phys. 46:4181-4195.
26. Schurtenberger, P., and R. C. Augusteyn. 1991. Structural properties of polydisperse biopolymer solutions: a light scattering study of bovine α-crystallin. Biopolymers. 31:1229-1240.
27. Siezen, R. J., and H. Berger. 1978. The quaternary structure of bovine α-crystallin. Size and shape studies by sedimentation, small-angle x-ray scattering and quasi-elastic light scattering. Eur. J. Biochem. 91: 397-405.
28. Spector, A., R. Chiesa, J. Sredy, and W. Garner. 1985. cAMP-dependent phosphorylation of bovine lens α-crystallin. Proc. Natl. Acad. Sci. USA. 82:4712-4716.
29. Tardieu, A., D. Laporte, P. Licinio, B. Krop, and M. Delaye. 1986. Calf lens α-crystallin quaternary structure. A three-layer tetrahedral model. J. Mol. Biol. 192:711-724.
30. Tardieu, A., D. Laporte, and M. Delaye. 1987. Colloidal dispersions of α-crystallin proteins. I. Small angle X-ray analysis of the dispersion structure. J. Physique. 48:1207-1215.
31. 2 chain of bovine α-crystallin. Eur. J. Bioch. 39:207-222.
32. 2 chain of bovine α-crystallin. Eur. J. Biochem. 49:157-168.
33. van Haeringen, B., M. R. Van den Bogaerde, D. Eden, R. Van Grondelle, and M. Bloemendal. 1993. Further characterization of structural and electric properties of non-spherical α-crystallin. Eur. J. Biochem. 217: 143-150.
34. van Holde, K. E. 1985. Scattering. In Physical Biochemistry. Prentice-Hall Inc., Englewood Cliffs. 209-234.
35. van Iersel, J., J. F. Jzn, and J. A. Duine. 1985. Determination of absorption coefficients of purified proteins by conventional ultraviolet spectrophotometry and chromatography combined with multiwavelength detection. Anal. Biochem. 151:196-204.
36. van Kleef, F. S. M., W. W. de Jong, and H. J. Hoenders. 1975. Spetwise degradations and deamidation of the eye lens protein α-crystallin in ageing. Nature. 258:264-266.
37. van Veluwen, A., H. N. W. Lekkerkerker, C. G. de Kruif, and A. Vrij. 1988. Influence of polydispersity on dynamic light scattering measurements on concentrated solutions. J. Chem. Phys. 89:2810-2815.
38. Vérétout, F., M. Delaye, and A. Tardieu. 1989. Molecular basis of eye lens transparency. Osmotic pressure and x-ray analysis of α-crystallin solutions. J. Mol. Biol. 205:713-728.
39. Wang, X., and F. A. Bettelheim. 1989. Second virial coefficient of α-crystallin. Proteins. 5:166-169.
40. Wheale, R. A. 1974. Natural history of optics. In The Eye: Volume 6, Comparative Physiology. H. Davson and L.T. Graham, editors. Academic Press. New York. 36-41.
41. Xia, J. Z., T. Aerts, K. Donceel, and J. Clauwaert. 1994. Light scattering by bovine α-crystallin proteins in solution: hydrodynamic structure and interparticle interaction. Biophys. J. 66:861-872.
42. Yphantis, D. A. 1964. Equilibrium ultracentrifugation of dilute solutions. Biochemistry. 3:297-317.
43. Zamyatnin, A. A. 1972. Protein volume in solution. Prog. Biophys. Mol. Biol. 24:109-123.