Abstract
Two electrophoretic polymorphisms affecting lens crystallins, designated LEN-1 and LEN-2, have been discovered among inbred strains of mice. Analysis by isoelectric focusing demonstrated that both crystallins are monomeric proteins with isoelectric points at or above pH 7. Both proteins eluted in the low molecular weight (LM) fraction upon Sephadex G-200 gel filtration but LEN-2 was shown to be larger than LEN-1 by G75SF gel filtration and denaturing gel electrophoresis. Linkage analysis demonstrated that the genes encoding LEN-1 and LEN-2 assort independently. Amino acid analysis of the allelic products of the two genes revealed that genetic variants of each respective crystallin were very similar in amino acid compositions but that LEN-1 and LEN-2 were dissimilar crystallins.
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This research was sponsored in part by the Office of Health and Environmental Research, U.S. Department of Energy, under Contract DE-AC05-840R21400 with the Martin Marietta Energy Systems, Inc.
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Skow, L.C., Donner, M.E., Popp, R.A. et al. A second polymorphic lens crystallin (LEN-2) in the mouse: Genetic and biochemical analysis of LEN-1 and LEN-2. Biochem Genet 23, 181–189 (1985). https://doi.org/10.1007/BF00499122
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DOI: https://doi.org/10.1007/BF00499122