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Updated: Aug 11, 2026

Amide Hydrogen/Deuterium Exchange & MALDI-TOF Mass Spectrometry Analysis of Pak2 Activation
Published on: November 26, 2011
Identification of the peptide bond cleaved during activation of human C1r
Abstract:
CNBr cleavage of unreduced proenzyme C1r yielded fragment CP2b, isolated by gel filtration and high-pressure gel permeation chromatography. This fragment (approximately Mr 55 000) comprised at least 4 disulphide-linked peptides, which were separated by gel filtration after reduction and alkylation. Peptide CP2bRA4, overlapping the A- and B-chain regions in proenzyme C1r was digested by V8 staphylococcal protease, and the digest separated by reversed-phase HPLC. N-terminal sequence analysis of peptide CP2bRA4SP9 established that C1r activation involves the cleavage of a single Arg-Ile bond, located in the sequence: ... Gln-Arg-Gln-Arg-Ile-Ile-Gly-Gly ... .
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