A Second Polymorphic Lens Crystallin (LEN-2) in the Mouse: Genetic and Biochemical Analysis of LEN-1 and LEN-2

Overview

Journal Biochem Genet

Specialty Molecular Biology

Date 1985 Feb 1

PMID 3994658

Citations 3

Authors

L C Skow

M E Donner

R A Popp

E G Bailiff

Affiliations

Soon will be listed here.

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.

Citing Articles

Electrophoretic variation in low molecular weight lens crystallins from inbred strains of rats.

Donner M, Skow L, Kunz H, Gill 3rd T Biochem Genet. 1985; 23(9-10):787-800.

PMID: 3936479 DOI: 10.1007/BF02399409.

Mapping of mouse gamma crystallin genes on chromosome 1.

Skow L, Donner M, Huang S, Gardner J, Taylor B, Beamer W Biochem Genet. 1988; 26(9-10):557-70.

PMID: 3242494 DOI: 10.1007/BF02399601.

Assignment of the microtubule-associated protein 2 gene to mouse chromosome 1.

Lafuse W, Brown D, Zwilling B Mamm Genome. 1992; 3(1):48-51.

PMID: 1581633 DOI: 10.1007/BF00355843.

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