Bell C W, Fronk E, Gibbons I R
J Supramol Struct. 1979;11(3):311-7. doi: 10.1002/jss.400110305.
A high-resolution sodium dodecyl sulfate polyacrylamide gel electrophoresis system has been used to show the presence, in both whole sperm and isolated flagellar axonemes, of eight polypeptides migrating in the 300,000--350,000 molecular weight range characteristic of the heavy chains of dynein ATPase. Previously, only five such chains have been discernible. Extraction of isolated axonemes for 10 min at 4 degrees C with a solution containing 0.6 M NaCl, ph 7, releases a mixture of particles that separate, in sucrose density gradient centrifugation, into a major peak, dynein 1 ATPase, sedimenting at 21S and a minor peak at 12--14S. The polypeptide compositions of these two peaks are different. The dynein 1 peak, which contains most of the protein on the gradient, contains approximately equal quantities of two closely migrating heavy chains, with a small amount of a third, more slowly migrating chain; no other heavy chains appear in this peak. Two groups of smaller polypeptides (three intermediate chains, within the apparent molecular weight range 76,000--122,000 and four newly discovered light chains, within the apparent molecular weight range 14,000--24,000) cosediment with the 21S peak. The heavy chain composition of the 12--14S peak is more complex, all eight heavy chains occurring approximately the same ratios as occur in intact axonemes.
一种高分辨率十二烷基硫酸钠聚丙烯酰胺凝胶电泳系统已被用于显示，在整个精子和分离的鞭毛轴丝中，有8种多肽在300,000 - 350,000分子量范围内迁移，这是动力蛋白ATP酶重链的特征分子量范围。此前，只能辨别出5条这样的链。在4℃下用含0.6M NaCl、pH 7的溶液对分离的轴丝进行10分钟提取，会释放出一种颗粒混合物，在蔗糖密度梯度离心中，这些颗粒分离成一个主要峰，即动力蛋白1 ATP酶，沉降系数为21S，还有一个较小的峰，沉降系数在12 - 14S。这两个峰的多肽组成不同。动力蛋白1峰包含梯度上的大部分蛋白质，含有两条迁移紧密的重链，数量大致相等，还有少量第三条迁移较慢的链；该峰中没有其他重链出现。两组较小的多肽（三条中间链，表观分子量范围在76,000 - 122,000之间，以及四条新发现的轻链，表观分子量范围在14,000 - 24,000之间）与21S峰一起沉降。12 - 14S峰的重链组成更为复杂，所有8条重链出现的比例与完整轴丝中的大致相同。
