Ohtsuka S, Kimura S, Kawamura Y, Hirono Y, Maruyama K
Department of Biology, Faculty of Science, Chiba University, Japan.
Comp Biochem Physiol B. 1992 Nov;103(3):543-6. doi: 10.1016/0305-0491(92)90367-z.
Chicken leg gracilis muscle contained only alpha-connectin (ca 3000 kDa) without beta-connectin. When myofibrils were kept standing for 20 hr at 4 degrees C, alpha-connectin was degraded to beta-connectin (ca 2000 kDa) and 1200 kDa peptide. The latter was prepared from myofibrils and purified by gel filtration in the presence of SDS. A monoclonal antibody, alpha 7, to this 1200 kDa fragment was prepared. The antibody reacted with the 1200 kDa fragment and its mother molecule alpha-connectin, but not with beta-connectin. Immunoelectron microscopy using alpha 7, as well as other antibodies to chicken breast muscle beta-connectin, revealed that the 1200 kDa peptide covered the portion of alpha-connectin from the Z line to the N2 line region in the I band of chicken leg gracilis muscle sarcomeres. The results were in good agreement with those observed in rabbit skeletal muscle.
鸡腿股薄肌仅含有α-连接蛋白（约3000 kDa），而没有β-连接蛋白。当肌原纤维在4℃下放置20小时时，α-连接蛋白降解为β-连接蛋白（约2000 kDa）和1200 kDa的肽段。后者是从肌原纤维中制备的，并在SDS存在下通过凝胶过滤进行纯化。制备了针对该1200 kDa片段的单克隆抗体α7。该抗体与1200 kDa片段及其母分子α-连接蛋白反应，但不与β-连接蛋白反应。使用α7以及其他针对鸡胸肌β-连接蛋白的抗体进行免疫电子显微镜观察，结果显示1200 kDa的肽段覆盖了鸡腿股薄肌肌节I带中从Z线到N2线区域的α-连接蛋白部分。这些结果与在兔骨骼肌中观察到的结果非常一致。
