Rosenspire A J, Choi Y S
Mol Immunol. 1982 Dec;19(12):1515-26. doi: 10.1016/0161-5890(82)90262-0.
The myosin-affinity technique, along with conventional immunoaffinity chromatography of membrane immunoglobulin (mIg), was used to study the relation between proteins that bind to actin, and those that co-isolate with the mIg of normal chicken B-cells. In the case of biosynthetically-labeled cells, we found approximately 13 actin-associated polypeptides. Of this group, eight could be labeled with 125I surface labeling. When the actin-associated proteins were compared to proteins that co-isolate with mIg during immunoaffinity chromatography, we found that two of them (mol. wts 55,000 and 34,000) co-isolate with mIg. The 55,000 mol. wt polypeptide can be labeled with 125I surface labeling techniques, while the 34,000 mol. wt protein cannot, suggesting that only the 55,000 mol. wt protein is exposed on the outer surface of the plasma membrane. It is speculated that the function of these proteins may be involved in linking mIg to actin and perhaps to the cytoskeleton.
肌球蛋白亲和技术，连同传统的膜免疫球蛋白（mIg）免疫亲和层析法，被用于研究与肌动蛋白结合的蛋白质和那些与正常鸡B细胞的mIg共分离的蛋白质之间的关系。在生物合成标记细胞的情况下，我们发现了大约13种与肌动蛋白相关的多肽。在这一组中，有8种可以用125I表面标记法进行标记。当将与肌动蛋白相关的蛋白质与免疫亲和层析过程中与mIg共分离的蛋白质进行比较时，我们发现其中两种（分子量分别为55,000和34,000）与mIg共分离。分子量为55,000的多肽可以用125I表面标记技术进行标记，而分子量为34,000的蛋白质则不能标记，这表明只有分子量为55,000的蛋白质暴露在质膜的外表面。据推测，这些蛋白质的功能可能涉及将mIg与肌动蛋白以及可能与细胞骨架连接起来。
