A second polymorphic lens crystallin (LEN-2) in the mouse: genetic and biochemical analysis of LEN-1 and LEN-2

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 th...

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Veröffentlicht in:Biochemical genetics 1985-02, Vol.23 (1/2), p.181-189
Hauptverfasser: Skow, L.C, Donner, M.E, Popp, R.A, Bailiff, E.G
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Donner, M.E
Popp, R.A
Bailiff, E.G
description 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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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. 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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.</abstract><cop>New York, NY</cop><pub>Plenum Press</pub><pmid>3994658</pmid><doi>10.1007/BF00499122</doi><tpages>9</tpages></addata></record>
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ispartof Biochemical genetics, 1985-02, Vol.23 (1/2), p.181-189
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source MEDLINE; SpringerLink Journals - AutoHoldings
subjects Alleles
Amino Acid Sequence
Animals
Biological and medical sciences
Chromatography, Gel
Classical genetics, quantitative genetics, hybrids
Crystallins - analysis
Crystallins - genetics
Electrophoresis, Polyacrylamide Gel
EYES
Fundamental and applied biological sciences. Psychology
GENETICA
GENETICS
Genetics of eukaryotes. Biological and molecular evolution
GENETIQUE
Genotype
Isoelectric Focusing
Mice
Mice, Inbred Strains
Molecular Weight
OEIL
OJOS
Phenotype
POLIMORFISMO
POLYMORPHISM
Polymorphism, Genetic
POLYMORPHISME
Vertebrata
title A second polymorphic lens crystallin (LEN-2) in the mouse: genetic and biochemical analysis of LEN-1 and LEN-2
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