Heterogeneity of fast-oxidative muscle fibers of chicken demonstrated by anti-myosin monoclonal antibodies.
Heterogeneity of fast-oxidative muscle fibers of chicken demonstrated by anti-myosin monoclonal antibodies.
复制标题
抗肌球蛋白单克隆抗体证明鸡快速氧化肌纤维的异质性。
DOI：
10.1007/bf00492388
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发表时间：
1989
期刊：
影响因子：
--
通讯作者：
Shafiq,SA
中科院分区：
文献类型：
--
作者：
Zhang,Y;Lewis,SG;Shafiq,SA
应用肌球蛋白ATP酶组织化学染色和单克隆抗体免疫组化技术，对鸡两种快肌即内收肌（AS）和胸大肌（PM）的肌纤维型组成进行了研究。制备了两株抗鸡背阔肌前肌球蛋白（ALD）的单克隆抗体ALD-122和ALD-83，分别对肌球蛋白重链（MHC）和肌球蛋白轻链-1（myosin light chain-1，myosin light chain-1）具有特异性。它们与已报道的慢MHC（ALD-47）、快MHC（MF-14）和快轻链-2（MF-5）特异性单克隆抗体联用。ATP酶组织化学染色显示，AS肌和PM肌的大部分肌纤维分别呈IIA和IIB型。用抗MHC单克隆抗体ALD-122和MF-14免疫荧光染色，AS肌纤维呈明显的异质性，PM肌纤维呈均匀的免疫荧光反应。SDS-凝胶电泳和抗轻链单克隆抗体ALD-83免疫印迹分析也发现AS和PM肌球蛋白轻链组成的差异。这项研究清楚地表明，组织化学同质（IIA型）AS肌肉是由几个亚群的纤维，不同的肌球蛋白组成，这种异质性的肌肉是不是简单地由于存在变量的慢肌球蛋白在其纤维。
The fiber type composition of two fast muscles of the chicken, namely, adductor superficialis (AS) and pectoralis major (PM) was examined by the histochemical myosin ATPase staining and immunochemical techniques using monoclonal antibodies (McAbs). Two new McAbs produced against the myosin of the anterior latissimus dorsi (ALD) muscle of the chicken and named ALD-122 and ALD-83 were characterized to be specific for myosin heavy chain (MHC) and for myosin light chain-1 respectively. They were used in conjunction with previously reported McAbs specific for slow MHC (ALD-47), fast MHC (MF-14) and fast light chain-2 (MF-5). By the histochemical ATPase test most muscle fibers of AS and PM muscles reacted as IIA and IIB respectively. By immunofluorescent staining with the anti-MHC McAbs, ALD-122, and MF-14, the fibers of AS, muscle showed remarkable heterogeneity whereas PM muscle fibers reacted, uniformly. Differences in the myosin light chain composition of AS and PM muscles were also found by SDS-gel electrophoresis and immunoblot analysis with the anti-light chain McAb, ALD-83. The study clearly indicated that the histochemically homogenous (type IIA) AS muscle is composed of several subpopulations of fibers which differ in their myosin composition and that this heterogeneity of the muscle is not simply due to presence of variable amounts of slow myosin in its fibers.