Abstract:
:The calmodulin-like domain of calpain is important for the association of the calpain large and small subunits. We expressed the calmodulin-like domains of the large subunits of rabbit mu- and m-calpains and their small subunits in E. coli and purified them to homogeneity. Unlike the full-length subunits, the calmodulin-like domains are soluble in buffer containing Ca2+. We performed gel filtration chromatography of the purified proteins and found that all three calmodulin-like domains exist as homodimers in the absence of Ca2+ and dissociate into monomers upon the addition of Ca2+.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Suo S,Koike H,Sorimachi H,Ishiura S,Suzuki Kdoi
10.1006/bbrc.1999.0407subject
Has Abstractpub_date
1999-04-02 00:00:00pages
63-6issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(99)90407-2journal_volume
257pub_type
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