References
- Stark W. J., Sommer A., Smith R. E. Changing trends in intraocular lens implantation. Arch. Ophthalmol. 1989; 107: 1441–1444
- Kibbelaar M., Bloemendal H. The topography of lens proteins based on chromatography and two-dimensional gel electrophoresis. Exp. Eye Res. 1975; 21: 25–36
- Bloemendal H. Lens research: from protein to gene. Exp. Eye Res. 1985; 41: 429–448
- Garadi R., Katar M., Maisel H. Two-dimensional gel analysis of chick lens proteins. Exp. Eye Res. 1983; 36: 859–869
- Vidal P., Cabezas-Cerrato J. 2-D electrophoresis distribution of stable 14C-glycation products from pig lens crystallins in relation to diabetic cataract formation. Diabetes Res. Clin. Prac. 1989; 6: 233–236
- DeVries A. C.J., Vermeer M. A., Hendriks A. L.A.M., Bloemendal H., Cohen L. H. Biosynthetic capacity of the human lens upon aging. Exp. Eye Res. 1991; 53: 519–524
- Chylack L. T., Jr. Classification of human cataracts. Arch. Ophthalmol. 1978; 96: 888–892
- Zigler J. S., Jr., Horwitz J., Kinoshita J. H. The human γ-crystallins I. Comparative studies on γ1, γ2, and γ3-crystallin. Exp. Eye Res. 1980; 31: 41–55
- O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 1975; 250: 4007–4021
- Anderson N. G., Anderson N. L. Analytical techniques for cell fractions. XXI. Two-dimensional analysis of serum and tissue proteins: Multiple isoelectric focusing. Anal. Biochem. 1978; 85: 331–341
- Anderson N. L., Anderson N. G. Analytical techniques for cell fractions. XXII. Two-dimensional analysis of serum and tissue proteins: Multiple gradient-slab gel electrophoresis. Anal. Biochem. 1978; 85: 341–354
- O'Farrell P. Z., Goodman H. M., O'Farrell P. H. High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 1977; 12: 1133–1142
- Neuhoff V., Arold N., Taube D., Ehrhardt W. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 1988; 9: 255–262
- Vermorken F. J.M., Herbrink P., Bloemendal H. Synthesis of lens protein in vitro.-formation of beta-crystallin. Eur. J. Biochem. 1977; 78: 617–622
- Slingsby C., Driessen H. P.C., Mahadevan D., Bax B., Blundell T. L. Evolutionary and functional relationships between the basic and acidic β-crystallins. Exp. Eye Res. 1988; 46: 375–403
- Dubin R. A., Ally A. H., Chung S., Piatigorsky J. Human αβ-crystallin gene and preferential promoter function in lens. Genomics 1990; 7: 594–601
- McDevitt D. S., Hawthins J. W., Jaworski C. J., Piatigorsky J. Isolation and partial characterization of the human αA-crystallin gene. Exp. Eye Res. 1986; 43: 285–291
- de Jong W. W., Gleaves J. T., Boulter D. Evolutionary changes of α-crystallin and the phytogeny of mammalian orders. J. Mol. Evol. 1977; 10: 123–135
- Alcala J., Katar M., Rudner G., Maisel H. Human beta-crystallins: regional and age related changes. Curr. Eye Res. 1988; 7: 353–359
- Ringens P. J., Hoenders H. J., Bloemendal H. Protein distribution and characterization in the prenatal and postnatal human lens. Exp. Eye Res. 1982; 34: 815–823
- Thomson J. A., Augusteyn R. C. Ontogeny of human lens crystallins. Exp. Eye Res. 1985; 40: 393–410
- Zigler J. S., Jr., Russell P., Takemoto L. J., Schwab S. J., Hansen J. S., Horwitz J., Kinoshita J. H. Partial characterization of three distinct populations of human γ-crystallins. Invest. Ophthalmol. Vis. Sci. 1985; 26: 525–531
- Takemoto L., Straatsma B., Horwitz J. Immunochemical characterization of the major low molecular weight polypeptide (10K) from human cataractous lenses. Exp. Eye Res. 1989; 48: 261–270
- Srivastava O. P. Age-related increase in concentration and aggregation of degraded polypeptides in human lenses. Exp. Eye Res. 1988; 47: 525–543