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

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.

authors

• Skow, Loren

published proceedings

• Biochem Genet

author list (cited authors)

• Skow, L. C., Donner, M. E., Popp, R. A., & Bailiff, E. G.

citation count

• 10

complete list of authors

• Skow, LC||Donner, ME||Popp, RA||Bailiff, EG

publication date

• February 1985

publisher

• Springer Nature  Publisher

keywords

• Alleles
• Amino Acid Sequence
• Animals
• Chromatography, Gel
• Crystallins
• Electrophoresis, Polyacrylamide Gel
• Genotype
• Isoelectric Focusing
• Mice
• Mice, Inbred Strains
• Molecular Weight
• Phenotype
• Polymorphism, Genetic

PubMed Central ID

• 3994658

Digital Object Identifier (DOI)

• 10.1007/BF00499122

start page

• 181

end page

• 189

volume

• 23

issue

• 1-2

URL

• http://dx.doi.org/10.1007/bf00499122