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Updated: Mar 19, 2026
LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
Published on: April 9, 2017
Improved Purification and Spectroscopic Properties of Squash Glutamate Decarboxylase
T Matsumoto1, I Yamaura1, M Funatsu1
1a Department of Applied Microbial Technology , The Kumamoto Institute of Technology , Kumamoto 860 , Japan.
Abstract:
Squash glutamate decarboxylase was purified by DEAE-Cellulose batchwise followed by Blue-Sepharose, Cellulofine GCL-2000, and Toyopearl HW-55F column chromatography. The purified glutamate decarboxylase had a high specific activity (95.0 u/mg). The absorption spectrum of glutamate decarboxylase had an absorption maximum at 420 nm in the range 300-500 nm. A pH change from 5.3 to 7.8 was accompanied by a decrease in absorbancy at 420 nm. One mole of glutamate decarboxylase contained 3.8 and 1.3 mol of pyridoxal 5'-phosphate at pH 5.8 and pH 7.8, respectively.
