Purification and characterization of a calcium-activated neutral protease from rabbit skeletal muscle which requires calcium ions of microM order concentration.

@article{Inomata1983PurificationAC,
  title={Purification and characterization of a calcium-activated neutral protease from rabbit skeletal muscle which requires calcium ions of microM order concentration.},
  author={Mitsushi Inomata and Masahiro Hayashi and Mitsuhiro Nakamura and Kazutomo Imahori and Seiichi Kawashima},
  journal={Journal of biochemistry},
  year={1983},
  volume={93 1},
  pages={
          291-4
        }
}
One form of calcium-activated neutral protease (CANP) highly sensitive to calcium ions was purified by column chromatographic procedures to homogeneity. The purified enzyme required microM order Ca2+ (mu CANP), and the half-maximum activity was attained at 50 microM Ca2+. The electrophoretic mobility in a non-denaturing buffer showed that this enzyme is less acidic than another CANP which required mM order Ca2+ (mCANP). On SDS-polyacrylamide gel electrophoresis, the enzyme separated into two… CONTINUE READING

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