Ontology highlight
ABSTRACT:
SUBMITTER: Croall DE
PROVIDER: S-EPMC2646846 | biostudies-literature | 2008 Nov
REPOSITORIES: biostudies-literature
Croall Dorothy E DE Vanhooser Lisa M LM Cashon Robert E RE
Biochimica et biophysica acta 20080828 11
The specific, calcium-dependent, high affinity interaction between calpain and its endogenous inhibitor calpastatin was exploited to selectively detect the calcium-bound, catalytically competent, conformation of calpain in vitro. Modification of calpastatin domain-1 (Val(114)-Ser(270)) or its N-terminal fragment (Val(114)-Pro(202)), at selected unique cysteine residues with maleimide-AlexaFluor546 did not compromise calpastatin function (inhibition of calpain) or its binding with calpain. Ca(2+) ...[more]