Subunit composition of rodent isomyosins and their distribution in hindlimb skeletal muscles.
Subunit composition of rodent isomyosins and their distribution in hindlimb skeletal muscles.
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啮齿动物同肌球蛋白的亚基组成及其在后肢骨骼肌中的分布。
DOI：
10.1152/jappl.1987.63.5.2101
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Baldwin,KM
中科院分区：
文献类型：
--
作者：
Tsika,RW;Herrick,RE;Baldwin,KM
三个成人骨骼肌肌节肌球蛋白重链（MHC）基因已被确定在大鼠中，这表明表达的天然肌球蛋白亚型可以区分，在某种程度上，根据其MHC组成。本研究旨在确定5种主要的天然异肌球蛋白[3种快速（Fm 1，Fm 2，Fm 3），1种慢速（Sm）和1种中间（Im）]，通常在成年大鼠后肢骨骼肌的频谱中表达，除了它们的轻链组成外，还可以根据它们的MHC谱进一步区分。结果表明，在肌肉组成的快速收缩糖酵解（FG）纤维和组成的Fm 1，Fm 2，和Fm 3，如阔筋膜张肌，只有一个MHC，指定为快速IIb型，可以解决。在比目鱼肌，包括慢收缩氧化和快收缩氧化糖酵解纤维和表达Sm和Im，两个MHC带被解决，并指定为慢/心脏β-MHC和快IIa型MHC。在表达所有三种纤维类型的混合物和完全互补的异肌球蛋白的肌肉中，如在跖肌中所见，MHC可以被分解成三条带。轻链的特点是每种肌肉类型，以及纯化的异肌球蛋白。这些数据表明，Im（IIa）由快和慢轻链的混合物组成，而Fm（IIb）和Sm（β）亚型分别仅由快型和慢型轻链组成。从表达对比异构体表型的肌肉中提取的变性肌球蛋白的多肽图谱表明慢肌球蛋白、中间肌球蛋白和快肌球蛋白同种型之间的MHC一级结构的差异。这些发现表明：1）Fm、Im和Sm异构体根据其重链和轻链组分进行分化; 2）每种异肌球蛋白以特征性方式分布在大鼠后肢骨骼肌中。此外，这些数据表明，在给定的肌肉或肌肉区域中的异肌球蛋白的比例对肌肉活动期间该肌肉的功能具有生理重要性。
Three adult skeletal muscle sarcomeric myosin heavy chain (MHC) genes have been identified in the rat, suggesting that the expressed native myosin isoforms can be differentiated, in part, on the basis of their MHC composition. This study was undertaken to ascertain whether the five major native isomyosins [3 fast (Fm1, Fm2, Fm3), 1 slow (Sm), and 1 intermediate (Im)], typically expressed in the spectrum of adult rat skeletal muscles comprising the hindlimb, could be further differentiated on the basis of their MHC profiles in addition to their light chain composition. Results show that in muscles comprised exclusively of fast-twitch glycolytic (FG) fibers and consisting of Fm1, Fm2, and Fm3, such as the tensor fasciae latae, only one MHC, designated as fast type IIb, could be resolved. In soleus muscle, comprised of both slow-twitch oxidative and fast-twitch oxidative-glycolytic fibers and expressing Sm and Im, two MHC bands were resolved and designated as slow/cardiac beta-MHC and fast type IIa MHC. In muscles expressing a mixture of all three fiber types and a full complement of isomyosins, as seen in the plantaris, the MHC could be resolved into three bands. Light chain profiles were characterized for each muscle type, as well as for the purified isomyosins. These data suggest that Im (IIa) consists of a mixture of fast and slow light chains, whereas Fm (IIb) and Sm (beta) isoforms consist solely of fast- and slow-type light chains, respectively. Polypeptide mapping of denatured myosin extracted from muscles expressing contrasting isoform phenotypes suggests differences in the MHC primary structure between slow, intermediate, and fast myosin isotypes. These findings demonstrate that 1) Fm, Im, and Sm isoforms are differentiated on the bases of both their heavy and light chain components and 2) each isomyosin is distributed in a characteristic fashion among rat hindlimb skeletal muscles. Furthermore, these data suggest that the ratio of isomyosins in a given muscle or muscle region is of physiological importance to the function of that muscle during muscular activity.
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大鼠肝癌细胞和大鼠肝脏中铁蛋白的生物合成。
影响因子：
4.8
作者：
S. S. Lee;G. Richter
通讯作者：
G. Richter
溶酶体蛋白酶的内源性抑制剂。
DOI：
--
发表时间：
1983
影响因子：
11.1
作者：
S. Pontremoli;E. Melloni;F. Salamino;B. Sparatore;M. Michetti;B. Horecker
通讯作者：
B. Horecker
通过免疫荧光原位检测细胞内铁蛋白的蛋白质亚基。
影响因子：
6
作者：
J. C. Lee;S. S. Lee;K. Schlesinger;G. Richter
通讯作者：
G. Richter
淋巴组织中的溶酶体。
DOI：
--
发表时间：
1967
期刊：
影响因子：
--
作者：
W. Bowers;J. Finkenstaedt;C. Duve
通讯作者：
C. Duve
DOI：
--
发表时间：
1968-06
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
J. Coffey;C. D. Duve
通讯作者：
J. Coffey;C. D. Duve