Lieska N, Chen J, Maisel H, Romero-Herrera A E
Biochim Biophys Acta. 1980 Nov 20;626(1):136-53. doi: 10.1016/0005-2795(80)90205-6.
The intermediate filaments from the bovine ocular lens can be fractionated into three 54000 dalton polypeptides (alpha, beta and gamma) which are present in equimolar quantities and differ from one another with respect to isoelectric point, two-dimensional peptide map pattern and total amino acid composition. The polypeptides, for which the name lentin is proposed, were purified from the 8 M urea extract of the water-insoluble residue of the cortical fiber cells by ion-exchange chromatography on DE- and CM-cellulose. The regeneration of native-appearance filaments from each purified fraction, or combinations thereof, definitively established the three polypeptides as the subunit species. Additionally, small diameter 'protofilaments' were regenerated when one or two fractions were utilized, but not when all three fractions were combined. This, together with the fact that the stoichiometric yield of the three species was invariably equimolar, suggests that alpha, beta, and gamma may be distinct entities not related by artifactual interconversion.
牛眼晶状体的中间丝可被分离成三种分子量为54000道尔顿的多肽（α、β和γ），它们以等摩尔量存在，在等电点、二维肽图模式和总氨基酸组成方面彼此不同。我们建议将这些多肽命名为lentin，它们是通过在DE - 和CM - 纤维素上进行离子交换色谱法，从皮质纤维细胞水不溶性残渣的8M尿素提取物中纯化得到的。从每个纯化组分或其组合中再生出具有天然外观的丝，明确确定这三种多肽为亚基种类。此外，当使用一种或两种组分时可再生出小直径的“原丝”，但当三种组分全部组合时则不能。这一点，再加上这三种种类的化学计量产率始终为等摩尔的事实，表明α、β和γ可能是不同的实体，并非通过人为的相互转化而相关。
