Clark T G, Rosenbaum J L
Cell. 1979 Dec;18(4):1101-8. doi: 10.1016/0092-8674(79)90223-x.
The nuclear gel of Xenopus oocytes contains a meshwork of randomly oriented microfilaments which have been identified as F-actin by decoration with rabbit skeletal muscle myosin subfragment-1 (S-1). Nuclear gel preparations treated with S-1 differ in several respects from control preparations incubated in either aqueous medium alone, or medium containing BSA. Actin filaments in control preparations appear less well preserved than those in S-1 treated preparations of the nuclear gel. The nucleoli of control preparations are extremely dense, while those of S-1 treated preparations have a more open, granular appearance. Large granular aggregates, which are a prominent feature of the controls, are seen much less frequently in S-1-treated preparations of the nuclear gel. These morphological differences appear to be correlated with the binding of protein to F-actin, since nuclear gel preparations incubated in tropomyosin, which also binds to actin filaments, appear similar to those treated with S-1. Approximately 63% of the total nuclear actin exists in a globular state, while 37% is filamentous.
非洲爪蟾卵母细胞的核凝胶含有由随机取向的微丝组成的网络，通过用兔骨骼肌肌球蛋白亚片段-1（S-1）进行标记，这些微丝已被鉴定为F-肌动蛋白。用S-1处理的核凝胶制剂在几个方面与单独在水性介质或含有牛血清白蛋白的介质中孵育的对照制剂不同。对照制剂中的肌动蛋白丝似乎不如核凝胶的S-1处理制剂中的保存得好。对照制剂的核仁极其致密，而S-1处理制剂的核仁具有更开放的颗粒状外观。大颗粒聚集体是对照的一个突出特征，在核凝胶的S-1处理制剂中很少见到。这些形态学差异似乎与蛋白质与F-肌动蛋白的结合有关，因为在原肌球蛋白中孵育的核凝胶制剂，原肌球蛋白也与肌动蛋白丝结合，其外观与用S-1处理的制剂相似。总的核肌动蛋白中约63%以球状存在，而37%是丝状的。
