Abstract:
:The hypothesis that calpain subunits dissociate in the presence of Ca2+ has been tested by methods which avoid interference by Ca2+-induced aggregation and large subunit autolysis. Inactive Cys105Ser-m-calpain, bound either to Ni-NTA-agarose or to immobilized casein, after incubation with Ca2+, could be recovered in high yield as a heterodimer. Natural bovine m-calpain, after irreversible inhibition with Z-LLY-CHN2, also bound to immobilized casein and was eluted as a heterodimer. The Ca2+ requirements of calpain containing a small subunit with EF-hand mutations were higher, both before and after autolysis, than those of wild-type calpain. In mixtures of wild-type and mutant enzymes, subunit exchange did not occur in the presence of Ca2+. The results demonstrate that the subunits in both natural and recombinant m-calpain, in the given experimental conditions, remain associated in the presence of Ca2+ both before and after autolysis.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Dutt P,Arthur JS,Croall DE,Elce JSdoi
10.1016/s0014-5793(98)01167-3subject
Has Abstractpub_date
1998-10-09 00:00:00pages
367-71issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01167-3journal_volume
436pub_type
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