| Literature DB >> 12871716 |
Stifun Mittoo1, Lars E Sundstrom, Mark Bradley.
Abstract
Two new probes for the detection of calpain I activity based on fluorescence resonance energy transfer technology have been synthesized and evaluated. The probes incorporated the cleavage site present in alpha-spectrin, a naturally occurring substrate of calpain I. The design of the internally quenched substrates is such that the calpain-sensitive bond of the peptides (between the Tyr-Gly residues) is located centrally between the donor and the quencher chromophores. The calpain assay protocol is capable of detecting enzymatic activity in the nanomolar region.Entities:
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Year: 2003 PMID: 12871716 DOI: 10.1016/s0003-2697(03)00324-5
Source DB: PubMed Journal: Anal Biochem ISSN: 0003-2697 Impact factor: 3.365