Biral D, Volpe P, Damiani E, Margreth A
Centro di Studio per la Biologia e la Fisiopatologia Muscolare del CNR, Università di Padova, Italy.
FEBS Lett. 1992 Mar 9;299(2):175-8. doi: 10.1016/0014-5793(92)80241-8.
The cardiac and skeletal muscle isoforms of calsequestrin (CS), the low affinity, high capacity Ca2+ binding protein localized in the lumen of sarcoplasmic reticulum, are the products of two different genes (Fliegel, L., Leberer, E., Green, N.M. and MacLennan, D.H. (1982) FEBS Lett. 242, 297-300), and can be both purified from slow-twitch skeletal muscle of the rabbit (Damiani, E., Volpe, P. and Margreth, A. (1990) J. Muscle Res. Cell Motil. 11, 522-530). Here we show that both CS isoforms coexist in slow-twitch muscle fibers as indicated by indirect immunofluorescent staining of cryosections with affinity-purified antibodies specific for each CS isoform.
肌集钙蛋白(CS)的心肌和骨骼肌异构体是两种不同基因的产物,CS是一种低亲和力、高容量的Ca2+结合蛋白,定位于肌浆网腔中(弗利格尔,L.,莱贝雷尔,E.,格林,N.M.和麦克伦南,D.H.(1982年)《欧洲生物化学学会联合会快报》242,297 - 300),并且两者都可以从兔的慢肌骨骼肌中纯化得到(达米亚尼,E.,沃尔佩,P.和玛格雷思,A.(1990年)《肌肉研究与细胞运动杂志》11,522 - 530)。在这里我们表明,如用针对每种CS异构体的亲和纯化抗体对冷冻切片进行间接免疫荧光染色所示,两种CS异构体共存于慢肌纤维中。