Abstract
The Ca2+ binding properties of calpain are of great interest, both biochemically in the wider context of EF-hand proteins, and physiologically, in the context of calpain regulation. There are two major parameters which one might wish to measure: the actual number of binding sites (n) and the binding constants for Ca2+. The latter is normally the macroscopic binding constant for Ca2+ of the molecule as a whole (Kd), or the microscopic binding constants for each of the EF-hands, but for cooperative binding these are much more difficult to measure. There is evidence of various kinds to suggest that Ca2+ binding causes conformational change in the whole molecule, and this forms the basis for measuring Ca2+ binding by means of changes in fluorescence.
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© 2000 Humana Press Inc.
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Arthur, J.S.C., Elce, J.S. (2000). Fluorescence Measurements of Ca2+ Binding to Domain VI of Calpain. In: Elce, J.S. (eds) Calpain Methods and Protocols. Methods in Molecular Biology™, vol 144. Humana Press. https://doi.org/10.1385/1-59259-050-0:121
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DOI: https://doi.org/10.1385/1-59259-050-0:121
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