Kibbelaar M A, Selten-Versteegen A M, Dunia I, Benedetti E L, Bloemendal H
Eur J Biochem. 1979 Apr;95(3):543-9. doi: 10.1111/j.1432-1033.1979.tb12995.x.
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.
本文提供的证据表明，小牛晶状体水溶性部分的一种蛋白质成分能与脱氧核糖核酸酶I（DNAse I）特异性结合。基于这一特性，该多肽可通过应用DNAse I亲和层析进行纯化。与此同时，一种分子量为55000的蛋白质和相当大量的α-晶状体蛋白与这种分子量为42000的多肽共同纯化。通过用2-（[三（羟甲基）甲基]氨基）乙磺酸提取小牛晶状体的水不溶性部分，然后进行凝胶过滤，也获得了高度纯化的42000-Mr蛋白质。氨基酸分析、肽图谱分析和电子显微镜显示，从晶状体两个部分获得的蛋白质与非肌肉肌动蛋白相同。此外，55000-Mr蛋白质的氨基酸组成与猪胃骨骼蛋白相同，与小牛脑结蛋白非常相似。
