Open AccessActin in Mammalian Lens
Author(s) -
KIBBELAAR Mac A.,
SELTENVERSTEEGEN AnneMarie E.,
DUNIA Irène,
BENEDETTI E. Lucio,
BLOEMENDAL Hans
Publication year - 1979
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1979.tb12995.x
Subject(s) - biochemistry , actin , tris , size exclusion chromatography , amino acid , peptide , hydroxymethyl , biology , chemistry , enzyme , stereochemistry
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 M r 55000 and a rather large amount of α‐crystallin copurify with this polypeptide, which has a molecular weight of 42000. Highly purified 42000‐ M r 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‐ M r protein is identical to hog stomach skeletin and very similar to calf brain desmin.