PMID: 2096909Aug 1, 1990Paper

Effects of calcium and calmodulin antagonists on calpain II subunit conformations

International Journal of Biological Macromolecules
H HongS C el-Saleh

Abstract

Only the 80-kD catalytic subunit of smooth muscle calpain II shows a change in intrinsic fluorescence on binding calcium, but both the 80-kD and 30-kD subunits show fluorescence changes in bound toluidinyl-naphthalenesulphonate as a result of calcium binding. Both subunits also show changes in intrinsic fluorescence in the presence of calmidazolium and felodipine. These studies indicate that both subunits have binding sites for calcium and the calmodulin antagonists, which are probably located in the calmodulin-like domain of each subunit.

References

Aug 1, 1979·The Biochemical Journal·A J BarrettC A Sayers
Jan 1, 1990·The International Journal of Biochemistry·H HongP Johnson
Mar 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·S PontremoliB L Horecker
Jan 1, 1985·Current Topics in Cellular Regulation·S PontremoliB L Horecker
Feb 1, 1988·The Biochemical Journal·J A Cox
Nov 1, 1984·Archives of Biochemistry and Biophysics·T KikuchiT Murachi

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Citations

Mar 17, 2019·Cellular and Molecular Life Sciences : CMLS·Antonio VillaloboMartin W Berchtold

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