Actin in mammalian lens.
In this paper evidence is provided that one of the protein components of the water-soluble fraction of the calf lens binds specifically to deoxyribonuclease I (DNAse I). On the basis of this property, the polypeptide could be purified by applying DNAse I affinity chromatography. Concomitantly a protein of Mr55000 and a rather large amount of alpha-crystallin copurify with this polypeptide, which has a molecular weight of 42000. Highly purified 42000-Mr protein was also obtained by extraction of the water-insoluble fraction of the calf lens with 2-([tris(hydroxymethyl)methyl]amino) ethanesulfonic acid followed by gel filtration. Amino acid analyses, peptide mapping and electron microscopy show that the protein obtained from both lens fractions is identical to non-muscle actin. Furthermore the amino acid composition of the 55000-Mr protein is identical to hog stomach skeletin and very similar to calf brain desmin.
D000199:Actins / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002462:Cell Membrane / Q000648:ultrastructure; D002846:Chromatography, Affinity; D003851:Deoxyribonucleases; D007908:Lens, Crystalline / Q000032:analysis*; D008970:Molecular Weight; D013045:Species Specificity; D013552:Swine
D000199:Actins; D000596:Amino Acids; D003851:Deoxyribonucleases