Abe M, Mizuno T, Nishida W, Hiwada K
Second Department of Internal Medicine, Ehime University School of Medicine, Japan.
Biochem Int. 1992 Oct;28(2):249-54.
Five mouse monoclonal antibodies, CaD 1-5, against chicken gizzard caldesmon were prepared. One of them (CaD4) was characterized by means of immunoblotting and its effect on actomyosin Mg(2+)-ATPase activity. CaD4 recognized the tropomyosin-binding site of caldesmon. CaD4 reversed the caldesmon-induced inhibition of actomyosin Mg(2+)-ATPase activity in a dose-dependent manner. These results suggest that the epitope recognized by CaD4 is an important domain for the function of caldesmon on the actinmyosin interaction in the smooth muscle contraction-relaxation system.
制备了五种针对鸡砂囊钙调蛋白的小鼠单克隆抗体CaD 1 - 5。其中一种(CaD4)通过免疫印迹法进行了表征,并研究了其对肌动球蛋白Mg(2 +)-ATP酶活性的影响。CaD4识别钙调蛋白的原肌球蛋白结合位点。CaD4以剂量依赖性方式逆转了钙调蛋白对肌动球蛋白Mg(2 +)-ATP酶活性的抑制作用。这些结果表明,CaD4识别的表位是钙调蛋白在平滑肌收缩 - 舒张系统中肌动蛋白 - 肌球蛋白相互作用功能的重要结构域。