Fluorescence measurements of Ca2+ binding to domain VI of calpain

J. Simon C. Arthur, John S. Elce

    Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

    1 Citation (Scopus)


    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.

    Original languageEnglish
    Title of host publicationCalpain Methods and Protocols
    EditorsJohn S. Elce
    Place of PublicationTotowa, New Jersey
    PublisherHumana Press
    Number of pages7
    EditionPart II
    ISBN (Electronic)9781592590506
    ISBN (Print)9780896036321
    Publication statusPublished - 2000

    Publication series

    NameMethods in Molecular Biology
    PublisherHumana Press
    ISSN (Print)1064-3745
    ISSN (Electronic)1940-6029


    • Rats
    • Animals
    • Calcium
    • Spectrometry, Fluorescence
    • Recombinant Proteins
    • Kinetics
    • Calpain
    • Protein Structure, Tertiary
    • Protein Structure, Quaternary
    • Binding Sites


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