Sato C, Nishizawa K, Nakayama T, Nakamura H, Yoshimura N, Takano E, Murachi T
Cell Struct Funct. 1986 Sep;11(3):253-7. doi: 10.1247/csf.11.253.
Microtubule associated protein-1 of brain and its intracellular 350kd analogues were highly sensitive to purified Ca2+-dependent cysteine proteinase (calpain). After 15 second digestion, we detected intermediate degradation products of MAP-1 by immunoblotting using anti-MAP-1 antibody as 290, 260, 220, 170, 140, 112, 80, 68, and 32kd polypeptides. These values corresponded to the molecular weights of the immunoreactive polypeptides of microtubule-enriched cytoskeletons isolated from HeLa and SV-3Y1 cells, suggesting the action of endogenous calpain on intracellular MAP-1 analogues in vivo or during the course of preparation.
脑微管相关蛋白-1及其细胞内350kd类似物对纯化的钙依赖性半胱氨酸蛋白酶（钙蛋白酶）高度敏感。消化15秒后，我们用抗MAP-1抗体通过免疫印迹检测到MAP-1的中间降解产物，为290、260、220、170、140、112、80、68和32kd的多肽。这些数值与从HeLa和SV-3Y1细胞分离的富含微管的细胞骨架的免疫反应性多肽的分子量相对应，表明内源性钙蛋白酶在体内或制备过程中对细胞内MAP-1类似物的作用。
