Two different molecular species of pig calpastatin. Structural and functional relationship between 107 kDa and 68 kDa molecules.

@article{Takano1986TwoDM,
  title={Two different molecular species of pig calpastatin. Structural and functional relationship between 107 kDa and 68 kDa molecules.},
  author={Emiko Takano and Akio Kitahara and Tomoko Sasaki and Reiji Kannagi and Takashi Murachi},
  journal={The Biochemical journal},
  year={1986},
  volume={235 1},
  pages={
          97-102
        }
}
Calpastatin, the inhibitor protein acting specifically on calpain (EC 3.4.22.17; Ca2+-dependent cysteine proteinase), is known to be widely distributed in mammalian and avian cells. Two different molecular species of calpastatin were isolated and purified to homogeneity from pig heart muscle and from pig erythrocytes, and shown to be of 107 kDa and 68 kDa respectively on SDS/polyacrylamide-gel electrophoresis. Both calpastatins had very similar amino acid compositions when expressed as mol per… CONTINUE READING
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