Skow L C, Donner M E, Popp R A, Bailiff E G
Biochem Genet. 1985 Feb;23(1-2):181-9. doi: 10.1007/BF00499122.
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.
在近交系小鼠中发现了两种影响晶状体晶状体蛋白的电泳多态性，分别命名为LEN-1和LEN-2。等电聚焦分析表明，这两种晶状体蛋白均为单体蛋白，等电点在pH 7或以上。经Sephadex G-200凝胶过滤后，两种蛋白均在低分子量（LM）组分中洗脱，但通过G75SF凝胶过滤和变性凝胶电泳显示LEN-2比LEN-1更大。连锁分析表明，编码LEN-1和LEN-2的基因独立分离。对这两个基因的等位基因产物进行氨基酸分析发现，各自晶状体蛋白的遗传变体在氨基酸组成上非常相似，但LEN-1和LEN-2是不同的晶状体蛋白。
