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鸟类和哺乳动物慢肌的肌球蛋白轻链:种内多态性的证据。

Myosin light chains of avian and mammalian slow muscles: evidence of intraspecific polymorphism.

作者信息

Carraro U, dalla Libera L, Catani C

出版信息

J Muscle Res Cell Motil. 1981 Sep;2(3):335-42. doi: 10.1007/BF00713271.

DOI:10.1007/BF00713271
PMID:7287900
Abstract

The myosin light chains of slow muscles from different species have been examined two-dimensional gel electrophoresis. While the myosin light chain 2S of mammalian soleus muscles (rabbit, rat and guinea-pig) could not be distinguished from that of avian anterior latissimus dorsi (chicken and turkey), the 1S light chain complement of myosins shows inter- and intraspecific differences. The 1S light chain varies between birds and mammals. The 1S light chain is absent in avian slow myosins and has an electrophoretic mobility peculiar to each mammalian species. Furthermore the relative amount of 1S and 1S light chains varies in different muscles of the same mammalian species and among species.

摘要

已通过二维凝胶电泳对不同物种慢肌的肌球蛋白轻链进行了检测。虽然哺乳动物比目鱼肌(兔、大鼠和豚鼠)的肌球蛋白轻链2S与禽类背阔肌前部(鸡和火鸡)的无法区分,但肌球蛋白的1S轻链成分存在种间和种内差异。1S轻链在鸟类和哺乳动物之间有所不同。禽类慢肌肌球蛋白中不存在1S轻链,且每种哺乳动物的1S轻链都有其独特的电泳迁移率。此外,同一哺乳动物物种的不同肌肉以及不同物种之间,1S和2S轻链的相对含量也有所不同。

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Fast-white and fast-red isomyosins in guinea pig muscles.豚鼠肌肉中的快白和快红异肌球蛋白
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Myosin light chains of avian and mammalian slow muscles: peptide mapping of 2S light chains.鸟类和哺乳动物慢肌的肌球蛋白轻链:2S轻链的肽图谱分析
J Muscle Res Cell Motil. 1984 Aug;5(4):411-21. doi: 10.1007/BF00818259.
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The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定分子量的可靠性。
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