Kibbelaar M A, Ramaekers F C, Ringens P J, Selten-Versteegen A M, Poels L G, Jap P H, van Rossum A L, Feltkamp T E, Bloemendal H
Nature. 1980 Jun 12;285(5765):506-8. doi: 10.1038/285506a0.
Actin has been purified from varius non-muscle cells and characterized by its molecular weight and ability to polymerize into filaments. Although the occurrence of this protein has been postulated in the mammalian eye lens after observation of actin-like filaments in the electron microscope, definite (bio)chemical proof has been provided only recently. Amino acid analysis, peptide mapping and affinity chromatography revealed the identity of lens actin with the corresponding protein in other tissues. As the filaments could be obtained by co-isolation with highly purified lens plasma membranes, we were interested to know how the actin-containing structures wre located in situ. In the experimental approach reported here, the indirect immunofluorescence technique (IFT) was applied to unfixed cryostat sections of lens tissue. The distribution of actin in calf, rat and pigeon lens is described, and evidence from this for the role of actin in visual accommodation discussed.
肌动蛋白已从多种非肌肉细胞中纯化出来，并通过其分子量和聚合成细丝的能力进行了表征。尽管在电子显微镜下观察到类似肌动蛋白的细丝后，曾推测这种蛋白质存在于哺乳动物的眼晶状体中，但直到最近才提供了确切的（生物）化学证据。氨基酸分析、肽图谱分析和亲和层析揭示了晶状体肌动蛋白与其他组织中相应蛋白质的同一性。由于细丝可以通过与高度纯化的晶状体质膜共同分离而获得，我们很想知道含肌动蛋白的结构在原位是如何定位的。在本文报道的实验方法中，间接免疫荧光技术（IFT）被应用于晶状体组织的未固定低温切片。描述了肌动蛋白在小牛、大鼠和鸽子晶状体中的分布，并讨论了由此得出的肌动蛋白在视觉调节中作用的证据。
