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Current Eye Research Volume 5, 1986 - Issue 5
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Original Article

Further studies on low molecular weight crystalline: Relationship between the bovine βS the human 24kD protein and the γ-crystallins

J. S. Zigler Laboratory of Mechanisms of Ocular Diseases, National Eye Institute NIH, Bethesda, MD, 20892
,
P. Russell Laboratory of Mechanisms of Ocular Diseases, National Eye Institute NIH, Bethesda, MD, 20892
,
J. Horwitz Jules Stein Eye Institute, UCLA School of Medicine, Los Angeles, CA, 90024, USA
,
V. N. Reddy Eye Research Institute, Oakland University, Rochester, MI, 48063, USA
&
J. H. Kinoshita Laboratory of Mechanisms of Ocular Diseases, National Eye Institute NIH, Bethesda, MD, 20892
Pages 395-401 | Received 25 Feb 1986, Accepted 15 Apr 1986, Published online: 02 Jul 2009

References

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  • Zigler J. S., Jr., Russell P., Takernoto 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
  • van Dam A. F. Purification and composition studies of β3-crystallin. Exp. Eye Res 1966; 5: 255–266
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  • Driessen H. P.C., Herbrink P., Bloemendal H., de Jong W. W. The β-crystallin Bp chain is internally duplicated and homologous with γ-crystallin. Exp. Eye Res 1980; 31: 213–246
  • Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol. Chem 1969; 244: 1406–4112
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  • Gray W. R. End group analysis with dansyl chloride. “Methods in Enzymology” Vol XXV, C. H.W. Hirs, S. N. Timesheff. Academic Press, New York 1972; 121–138
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  • Kabasawa I., Kinoshita J. H., Barber G. W. Aging effects on the bovine lens γ-crystallins. Exp. Eye Res 1974; 18: 457–466
  • Kabasawa I., Tsunematsu Y., Barber G. W., Kinoshita J. H. Low molecular weight proteins of the bovine lenses. Exp. Eye Res 1977; 24: 437–448
  • Kabasawa I., Barber G. W., Kinoshita J. H. Aging effects and some properties on the human lens low molecular weight proteins. Jap. J. Ophthalmol 1977; 21: 87–97
  • Kabasawa I., Kodama T., Kabasawa M., Sakaue E., Watanabe M., Kimura M. Heterogeneity of human cataractous and normal lens γ-crystallins. Exp. Eye Res 1982; 35: 1–9
  • Harding J. J., Dilley K. J. Structural proteins of the mammalian lens: A review with emphasis on changes in development, aging and cataract. Exp. Eye Res 1976; 22: 1–73
  • Horwitz J., Ding L.-L., Cheung C.-C. The distribution of soluble crystalline in the nucleus of normal and cataractous human lenses. Lens Res 1983; 1: 159–174
  • Straatsma B. R., Horwitz J., Takemoto L. J., Lightfoot D. O., Ding L-L. Clinicobiochemical correlations in aging-related human cataract. Am. J. Ophthalmol 1984; 97: 457–469

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