Association and dissociation of the calcium-binding domains of calpain by Ca2+.

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+.

authors

Suo S,Koike H,Sorimachi H,Ishiura S,Suzuki K

doi

10.1006/bbrc.1999.0407

subject

Has Abstract

pub_date

1999-04-02 00:00:00

pages

63-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(99)90407-2

journal_volume

257

pub_type

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